polymyxin resistance

MetaCyc:PWY0-1338

The complete six-reaction native L-Ara4N-modified lipid A biosynthetic route, represented for Escherichia coli K-12. Starting at UDP-glucuronate, ArnA and ArnB form UDP-aminoarabinose; ArnA formylation, ArnC carrier transfer and ArnD deformylation supply the undecaprenyl-phosphate-linked donor used by ArnT to modify Kdo2-lipid A. The terminal source equation summarizes addition of two aminoarabinose residues, not a single elementary transfer or every cellular lipid species. ArnE and ArnF have jointly required transport-associated roles; no fixed heterodimer or energy-coupling mechanism is asserted. The older native hypothetical ArnD step is supported by later E. coli genetics and separately scoped purified Salmonella enzyme experiments. ArnA hexamer evidence is preparation-specific, and ArnB dimerization remains a similarity annotation. Resistance is conditional on pathway expression and the studied mutant or induction context; the record does not claim constitutive resistance of all K-12 cells. Upstream UDP-glucuronate and Kdo2-lipid A biosynthesis are outside this native boundary.

Pathway type
aminoarabinose lipid a modification
Organism scope

Read the source YAML

Pathway network

38 nodes · 50 asserted directed edges

Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.

Pathway network: polymyxin resistance 38 nodes · 50 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:58052 — consumes → RHEA:24703; Evidence: RHEA:24703consumes CHEBI:57540 — consumes → RHEA:24703; Evidence: RHEA:24703consumes RHEA:24703 — produces → CHEBI:58710; Evidence: RHEA:24703produces RHEA:24703 — produces → CHEBI:16526; Evidence: RHEA:24703produces RHEA:24703 — produces → CHEBI:57945; Evidence: RHEA:24703produces RHEA:24703 — part_of → MetaCyc:PWY0-1338; Evidence: MetaCyc:PWY0-1338, MetaCyc:RXN0-1861, RHEA:24703part of CHEBI:58710 — consumes → RHEA:24712; Evidence: RHEA:24712consumes CHEBI:29985 — consumes → RHEA:24712; Evidence: RHEA:24712consumes RHEA:24712 — produces → CHEBI:58708; Evidence: RHEA:24712produces RHEA:24712 — produces → CHEBI:16810; Evidence: RHEA:24712produces RHEA:24712 — part_of → MetaCyc:PWY0-1338; Evidence: MetaCyc:PWY0-1338, MetaCyc:RXN0-1863, RHEA:24712, RHEA:24712part of CHEBI:58708 — consumes → RHEA:24707; Evidence: RHEA:24707consumes CHEBI:195366 — consumes → RHEA:24707; Evidence: RHEA:24707consumes RHEA:24707 — produces → CHEBI:58709; Evidence: RHEA:24707produces RHEA:24707 — produces → CHEBI:57453; Evidence: RHEA:24707produces RHEA:24707 — produces → CHEBI:15378; Evidence: RHEA:24707produces RHEA:24707 — part_of → MetaCyc:PWY0-1338; The native folate participants are classes; current Rhea specifies the chemically balanced monoglutamate forms used for this reaction representation.; Evidence: MetaCyc:PWY0-1338, MetaCyc:RXN0-1862, RHEA:24707part of CHEBI:58709 — consumes → RHEA:27723; Evidence: RHEA:27723consumes CHEBI:60392 — consumes → RHEA:27723; Evidence: RHEA:27723consumes RHEA:27723 — produces → CHEBI:58909; Evidence: RHEA:27723produces RHEA:27723 — produces → CHEBI:58223; Evidence: RHEA:27723produces RHEA:27723 — part_of → MetaCyc:PWY0-1338; Evidence: MetaCyc:PWY0-1338, MetaCyc:RXN0-3521, RHEA:27723part of CHEBI:58909 — consumes → RHEA:27735; Evidence: RHEA:27735consumes CHEBI:15377 — consumes → RHEA:27735; Evidence: RHEA:27735consumes RHEA:27735 — produces → CHEBI:60463; Evidence: RHEA:27735produces RHEA:27735 — produces → CHEBI:15740; Evidence: RHEA:27735produces RHEA:27735 — part_of → MetaCyc:PWY0-1338; Native 22.5 marks this step hypothetical; later experiments support the transformation. E. coli gene-disruption evidence and purified Salmonella enzyme evidence are distinguished.; Evidence: MetaCyc:PWY0-1338, MetaCyc:RXN0-5409, RHEA:27735, PMID:37782650part of CHEBI:60463 — consumes → RHEA:35372; Evidence: RHEA:35372, PMID:11535605consumes CHEBI:58540 — consumes → RHEA:35372; Evidence: RHEA:35372consumes RHEA:35372 — produces → CHEBI:71399; Evidence: RHEA:35372produces RHEA:35372 — produces → CHEBI:60392; Evidence: RHEA:35372produces RHEA:35372 — part_of → MetaCyc:PWY0-1338; The current balanced equation represents two transfers to a Kdo-disaccharide-bearing lipid-A substrate. It does not impose double modification on every lipid-A molecule.; Evidence: MetaCyc:PWY0-1338, MetaCyc:RXN0-2001, RHEA:35372part of UniProtKB:P77398 — part_of → MetaCyc:CPLX0-7718; The named native hexamer represents the experimentally characterized assembly, not an exclusive oligomeric state or a claim that isolated domains are inactive.; Evidence: MetaCyc:CPLX0-7718, UniProtKB:P77398, PMID:15939024, PMID:31344437part of MetaCyc:CPLX0-7718 — catalyzes → RHEA:24703; NAD+ is a consumed and reduced substrate, not a permanently bound cofactor; ATP used in the crystal structure is a NAD+ mimic.; Evidence: MetaCyc:CPLX0-7718, UniProtKB:P77398, PMID:15807526, PMID:15939024catalyzes UniProtKB:P77690 — enables → RHEA:24712; Biosynthetic flux selects the Rhea right-to-left direction of a reversible aminotransferase. The functional gene-product role does not assert monomer sufficiency; the E. coli dimer annotation is by similarity.; Evidence: UniProtKB:P77690, PMID:12704196, UniProtKB:P77690enables MetaCyc:CPLX0-7718 — catalyzes → RHEA:24707; Folate is the formyl-donating substrate. Active isolated domains do not establish that a hexamer is mandatory for either chemistry.; Evidence: MetaCyc:CPLX0-7718, UniProtKB:P77398, PMID:15807526catalyzes UniProtKB:P77757 — enables → RHEA:27723; Functional E. coli ArnC role. The later Salmonella tetramer structure and Mn-containing assays are not evidence for a fixed E. coli oligomer or its physiological metal.; Evidence: UniProtKB:P77757, PMID:15695810, MetaCyc:G7167-MONOMER, PMID:39865303, PMID:37782650enables UniProtKB:P76472 — enables → RHEA:27735; E. coli activity assignment is supported by genetics plus the reviewed annotation and separately scoped Salmonella biochemistry. No E. coli physiological metal or fixed assembly is asserted.; Evidence: UniProtKB:P76472, PMID:37782650, PMID:37782650enables UniProtKB:P76473 — enables → RHEA:35372; Functional E. coli transferase role with native Kdo2-lipid-A substrate scope. The terminal equation is a two-transfer net reaction; the one-transfer lipid-IVA assay is an alternative substrate reaction, not this equation.; Evidence: MetaCyc:G7170-MONOMER, UniProtKB:P76473, PMID:11535604, PMID:17928292enables UniProtKB:P77690 — has_cofactor → CHEBI:597326; Evidence: UniProtKB:P77690, PMID:12704196has cofactor UniProtKB:Q47377 — enables → MetaCyc:PWY0-1338; Transport-associated pathway role jointly requiring ArnE and ArnF in the studied mutant background; neither edge asserts individual sufficiency, an established physical heterodimer, or direct catalysis of a glycosyltransfer reaction.; Evidence: UniProtKB:Q47377, PMID:17928292enables UniProtKB:P76474 — enables → MetaCyc:PWY0-1338; Transport-associated pathway role jointly requiring ArnE and ArnF in the studied mutant background; neither edge asserts individual sufficiency, an established physical heterodimer, or direct catalysis of a glycosyltransfer reaction.; Evidence: UniProtKB:P76474, PMID:17928292enables UniProtKB:P77757 — located_in → GO:0005886; Inner membrane mapped to the plasma-membrane cellular component; this does not locate the whole pathway in one compartment.; Evidence: UniProtKB:P77757located in UniProtKB:P76473 — located_in → GO:0005886; Inner membrane mapped to the plasma-membrane cellular component; this does not locate the whole pathway in one compartment.; Evidence: UniProtKB:P76473located in UniProtKB:P77690 — located_in → GO:0005829; Evidence: PMID:12704196located in RHEA:24703 — provides_input_for → RHEA:24712; The shared chemical class is CHEBI:58710.; Evidence: MetaCyc:PWY0-1338, RHEA:24703, RHEA:24712provides input for RHEA:24712 — provides_input_for → RHEA:24707; The shared chemical class is CHEBI:58708.; Evidence: MetaCyc:PWY0-1338, RHEA:24712, RHEA:24707provides input for RHEA:24707 — provides_input_for → RHEA:27723; The shared chemical class is CHEBI:58709.; Evidence: MetaCyc:PWY0-1338, RHEA:24707, RHEA:27723provides input for RHEA:27723 — provides_input_for → RHEA:27735; The shared chemical class is CHEBI:58909.; Evidence: MetaCyc:PWY0-1338, RHEA:27723, RHEA:27735provides input for RHEA:27735 — provides_input_for → RHEA:35372; The shared chemical class is CHEBI:60463. Donor transport by ArnE/ArnF is required between formation on the cytoplasmic side and ArnT utilization on the periplasmic side; this class-level edge is not direct substrate channeling.; Evidence: MetaCyc:PWY0-1338, RHEA:27735, RHEA:35372, PMID:17928292provides input for water; CHEBI:15377; Declared type: small_molecule small molecule water hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron formate; CHEBI:15740; Declared type: small_molecule small molecule formate carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide 2-oxoglutarate(2-); CHEBI:16810; Declared type: small_molecule small molecule 2-oxoglutarate(2-) (6R)-10-formyltetrahydrofolate(2-); CHEBI:195366; Declared type: small_molecule small molecule (6R)-10- formyltetrahydrofolate(2-) L-glutamate(1-); CHEBI:29985; Declared type: small_molecule small molecule L-glutamate(1-) (6S)-5,6,7,8-tetrahydrofolate(2-); CHEBI:57453; Declared type: small_molecule small molecule (6S)-5,6,7,8- tetrahydrofolate(2-) NAD(1-); CHEBI:57540; Declared type: small_molecule small molecule NAD(1-) NADH(2-); CHEBI:57945; Declared type: small_molecule small molecule NADH(2-) UDP-alpha-D-glucuronate(3-); CHEBI:58052; Declared type: small_molecule small molecule UDP-alpha-D-glucuronate(3-) UDP(3-); CHEBI:58223; Declared type: small_molecule small molecule UDP(3-) (Kdo)2-lipid A(6-) (E. coli); CHEBI:58540; Declared type: lipid lipid (Kdo)2-lipid A(6-) (E. coli) UDP-4-amino-4-deoxy-beta-L-arabinopyranose(1-); CHEBI:58708; Declared type: small_molecule small molecule UDP-4-amino-4-deoxy-beta-L- arabinopyranose(1-) UDP-4-deoxy-4-formamido-beta-L-arabinopyranose(2-); CHEBI:58709; Declared type: small_molecule small molecule UDP-4-deoxy-4-formamido- beta-L-arabinopyranose(2-) UDP-beta-L-threo-pentopyranos-4-ulose(2-); CHEBI:58710; Declared type: small_molecule small molecule UDP-beta-L-threo- pentopyranos-4-ulose(2-) 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate(1-); CHEBI:58909; Declared type: lipid lipid 4-deoxy-4-formamido-alpha-L- arabinopyranosyl ditrans,polycis-undecaprenyl phosphate(1-) ditrans,polycis-undecaprenyl phosphate(2-); CHEBI:60392; Declared type: lipid lipid ditrans,polycis-undecaprenyl phosphate(2-) 4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate zwitterion; CHEBI:60463; Declared type: lipid lipid 4-amino-4-deoxy-alpha-L- arabinopyranosyl ditrans,polycis-undecaprenyl phosphate zwitterion (beta-L-Ara4N)2-(KDO)2-lipid A(2-); CHEBI:71399; Declared type: lipid lipid (beta-L-Ara4N)2-(KDO)2-lipid A(2-) pyridoxal 5'-phosphate(2-); CHEBI:597326; Declared type: cofactor cofactor pyridoxal 5'-phosphate(2-) plasma membrane; GO:0005886; Declared type: cellular_component cellular component plasma membrane cytosol; GO:0005829; Declared type: cellular_component cellular component cytosol Bifunctional polymyxin resistance protein ArnA; UniProtKB:P77398; Declared type: protein protein Bifunctional polymyxin resistance protein ArnA UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase; UniProtKB:P77690; Declared type: protein protein UDP-4-amino-4-deoxy-L- arabinose--oxoglutarate aminotransferase Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase; UniProtKB:P77757; Declared type: protein protein Undecaprenyl-phosphate 4-deoxy-4-formamido-L- arabinose transferase Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD; UniProtKB:P76472; Declared type: protein protein Probable 4-deoxy-4-formamido-L- arabinose- phosphoundecaprenol deformylase ArnD Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase; UniProtKB:P76473; Declared type: protein protein Undecaprenyl phosphate- alpha-4-amino-4-deoxy-L- arabinose arabinosyl transferase Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE; UniProtKB:Q47377; Declared type: protein protein Probable 4-amino-4-deoxy-L- arabinose- phosphoundecaprenol flippase subunit ArnE Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF; UniProtKB:P76474; Declared type: protein protein Probable 4-amino-4-deoxy-L- arabinose- phosphoundecaprenol flippase subunit ArnF UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase; MetaCyc:CPLX0-7718; Declared type: complex complex UDP-4-amino-4-deoxy-L- arabinose formyltransferase/UDP- glucuronate dehydrogenase UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH; RHEA:24703; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo- pentopyranos-4-ulose + CO2 + NADH UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate; RHEA:24712; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity UDP-beta-L-threo- pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L- arabinose + 2-oxoglutarate UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+); RHEA:24707; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity UDP-4-amino-4-deoxy-beta-L- arabinose + (6R)-10- formyltetrahydrofolate => UDP-4-deoxy-4-formamido- beta-L-arabinose + (6S)- 5,6,7,8-tetrahydrofolate + H(+) UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP; RHEA:27723; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity UDP-4-deoxy-4-formamido- beta-L-arabinose + di- trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L- arabinopyranosyl di- trans,octa-cis-undecaprenyl phosphate + UDP 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate; RHEA:27735; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 4-deoxy-4-formamido-alpha-L- arabinopyranosyl di- trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L- arabinopyranosyl di- trans,octa-cis-undecaprenyl phosphate + formate 2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate; RHEA:35372; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 2 4-amino-4-deoxy-alpha-L- arabinopyranosyl di- trans,octa-cis-undecaprenyl phosphate + alpha- Kdo-(2->4)-alpha- Kdo-(2->6)-lipid A (E. coli) => (beta-L- Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis- undecaprenyl phosphate polymyxin resistance; MetaCyc:PWY0-1338; Declared type: pathway pathway polymyxin resistance

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli K-12
NCBITaxon:83333		taxon
water
CHEBI:15377		small molecule
hydron
CHEBI:15378		small molecule
formate
CHEBI:15740		small molecule
carbon dioxide
CHEBI:16526		small molecule
2-oxoglutarate(2-)
CHEBI:16810		small molecule
(6R)-10-formyltetrahydrofolate(2-)
CHEBI:195366		small molecule
L-glutamate(1-)
CHEBI:29985		small molecule
(6S)-5,6,7,8-tetrahydrofolate(2-)
CHEBI:57453		small molecule
NAD(1-)
CHEBI:57540		small molecule
NADH(2-)
CHEBI:57945		small molecule
UDP-alpha-D-glucuronate(3-)
CHEBI:58052		small molecule
UDP(3-)
CHEBI:58223		small molecule
(Kdo)2-lipid A(6-) (E. coli)
CHEBI:58540		lipid
UDP-4-amino-4-deoxy-beta-L-arabinopyranose(1-)
CHEBI:58708		small molecule
UDP-4-deoxy-4-formamido-beta-L-arabinopyranose(2-)
CHEBI:58709		small molecule
UDP-beta-L-threo-pentopyranos-4-ulose(2-)
CHEBI:58710		small molecule
4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate(1-)
CHEBI:58909		lipid
ditrans,polycis-undecaprenyl phosphate(2-)
CHEBI:60392		lipid
4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate zwitterion
CHEBI:60463		lipid
(beta-L-Ara4N)2-(KDO)2-lipid A(2-)
CHEBI:71399		lipid
pyridoxal 5'-phosphate(2-)
CHEBI:597326		cofactor
plasma membrane
GO:0005886		cellular component
cytosol
GO:0005829		cellular component
Bifunctional polymyxin resistance protein ArnA
UniProtKB:P77398		protein
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
UniProtKB:P77690		protein
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
UniProtKB:P77757		protein
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
UniProtKB:P76472		protein
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
UniProtKB:P76473		protein
Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE
UniProtKB:Q47377		protein
Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF
UniProtKB:P76474		protein
UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
MetaCyc:CPLX0-7718		complex
UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703		molecular activityleft to right
UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712		molecular activityright to left
UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707		molecular activityleft to right
UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723		molecular activityleft to right
4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735		molecular activityleft to right
2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372		molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
UDP-alpha-D-glucuronate(3-)
CHEBI:58052		consumes

UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703
  • RHEA:24703

    Source assertion: RHEA:24703 assigns CHEBI:58052 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24703']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24702_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24702_compound_3253']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3253)
NAD(1-)
CHEBI:57540		consumes

UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703
  • RHEA:24703

    Source assertion: RHEA:24703 assigns CHEBI:57540 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24703']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24702_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24702_compound_3484']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3484)
UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703		produces

UDP-beta-L-threo-pentopyranos-4-ulose(2-)
CHEBI:58710
  • RHEA:24703

    Source assertion: RHEA:24703 assigns CHEBI:58710 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24703']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24702_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24702_compound_5229']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5229)
UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703		produces

carbon dioxide
CHEBI:16526
  • RHEA:24703

    Source assertion: RHEA:24703 assigns CHEBI:16526 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24703']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24702_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24702_compound_4391']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_4391)
UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703		produces

NADH(2-)
CHEBI:57945
  • RHEA:24703

    Source assertion: RHEA:24703 assigns CHEBI:57945 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24703']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24702_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24702_compound_1650']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_1650)
UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703		part_of

MetaCyc:PWY0-1338
  • MetaCyc:PWY0-1338

    Source assertion: The native pathway explicitly includes RXN0-1861 in its six-reaction list.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-list/Reaction[@frameid="RXN0-1861"]
  • MetaCyc:RXN0-1861

    Source assertion: The native reaction carries the Rhea cross-reference 24703.

    Source location/ptools-xml/Reaction[@frameid="RXN0-1861"]/dblink[dblink-db="RHEA"]/dblink-oid
  • RHEA:24703

    Source assertion: Rhea master 24702 links directed reaction 24703; the selected orientation is left_to_right.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24702']/rh:directionalReaction[@rdf:resource='http://rdf.rhea-db.org/24703']
UDP-beta-L-threo-pentopyranos-4-ulose(2-)
CHEBI:58710		consumes

UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712
  • RHEA:24712

    Source assertion: RHEA:24712 assigns CHEBI:58710 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24712']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24710_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24710_compound_5229']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5229)
L-glutamate(1-)
CHEBI:29985		consumes

UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712
  • RHEA:24712

    Source assertion: RHEA:24712 assigns CHEBI:29985 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24712']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24710_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24710_compound_2079']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_2079)
UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712		produces

UDP-4-amino-4-deoxy-beta-L-arabinopyranose(1-)
CHEBI:58708
  • RHEA:24712

    Source assertion: RHEA:24712 assigns CHEBI:58708 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24712']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24710_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24710_compound_5232']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5232)
UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712		produces

2-oxoglutarate(2-)
CHEBI:16810
  • RHEA:24712

    Source assertion: RHEA:24712 assigns CHEBI:16810 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24712']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24710_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24710_compound_2975']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_2975)
UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712		part_of

MetaCyc:PWY0-1338
  • MetaCyc:PWY0-1338

    Source assertion: The native pathway explicitly includes RXN0-1863 in its six-reaction list.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-list/Reaction[@frameid="RXN0-1863"]
  • MetaCyc:RXN0-1863

    Source assertion: The native reaction carries the Rhea cross-reference 24713.

    Source location/ptools-xml/Reaction[@frameid="RXN0-1863"]/dblink[dblink-db="RHEA"]/dblink-oid
  • RHEA:24712

    Source assertion: Rhea master 24710 links directed reaction 24712; the selected orientation is right_to_left.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24710']/rh:directionalReaction[@rdf:resource='http://rdf.rhea-db.org/24712']
  • RHEA:24712

    Source assertion: Rhea master 24710 explicitly links native bidirectional cross-reference 24713 and the selected biosynthetic right-to-left reaction 24712.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24710']/rh:bidirectionalReaction; rh:directionalReaction
UDP-4-amino-4-deoxy-beta-L-arabinopyranose(1-)
CHEBI:58708		consumes

UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:58708 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_5232']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5232)
(6R)-10-formyltetrahydrofolate(2-)
CHEBI:195366		consumes

UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:195366 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_18717']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_18717)
UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707		produces

UDP-4-deoxy-4-formamido-beta-L-arabinopyranose(2-)
CHEBI:58709
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:58709 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_5231']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5231)
UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707		produces

(6S)-5,6,7,8-tetrahydrofolate(2-)
CHEBI:57453
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:57453 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_4996']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_4996)
UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707		produces

hydron
CHEBI:15378
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:15378 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_3249']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3249)
UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707		part_of

The native folate participants are classes; current Rhea specifies the chemically balanced monoglutamate forms used for this reaction representation.

MetaCyc:PWY0-1338
  • MetaCyc:PWY0-1338

    Source assertion: The native pathway explicitly includes RXN0-1862 in its six-reaction list.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-list/Reaction[@frameid="RXN0-1862"]
  • MetaCyc:RXN0-1862

    Source assertion: The native reaction carries the Rhea cross-reference 24707.

    Source location/ptools-xml/Reaction[@frameid="RXN0-1862"]/dblink[dblink-db="RHEA"]/dblink-oid
  • RHEA:24707

    Source assertion: Rhea master 24706 links directed reaction 24707; the selected orientation is left_to_right.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24706']/rh:directionalReaction[@rdf:resource='http://rdf.rhea-db.org/24707']
UDP-4-deoxy-4-formamido-beta-L-arabinopyranose(2-)
CHEBI:58709		consumes

UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723
  • RHEA:27723

    Source assertion: RHEA:27723 assigns CHEBI:58709 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27723']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27722_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27722_compound_5231']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5231)
ditrans,polycis-undecaprenyl phosphate(2-)
CHEBI:60392		consumes

UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723
  • RHEA:27723

    Source assertion: RHEA:27723 assigns CHEBI:60392 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27723']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27722_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27722_compound_6255']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6255)
UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723		produces

4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate(1-)
CHEBI:58909
  • RHEA:27723

    Source assertion: RHEA:27723 assigns CHEBI:58909 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27723']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27722_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27722_compound_5985']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5985)
UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723		produces

UDP(3-)
CHEBI:58223
  • RHEA:27723

    Source assertion: RHEA:27723 assigns CHEBI:58223 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27723']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27722_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27722_compound_2692']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_2692)
UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723		part_of

MetaCyc:PWY0-1338
  • MetaCyc:PWY0-1338

    Source assertion: The native pathway explicitly includes RXN0-3521 in its six-reaction list.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-list/Reaction[@frameid="RXN0-3521"]
  • MetaCyc:RXN0-3521

    Source assertion: The native reaction carries the Rhea cross-reference 27723.

    Source location/ptools-xml/Reaction[@frameid="RXN0-3521"]/dblink[dblink-db="RHEA"]/dblink-oid
  • RHEA:27723

    Source assertion: Rhea master 27722 links directed reaction 27723; the selected orientation is left_to_right.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27722']/rh:directionalReaction[@rdf:resource='http://rdf.rhea-db.org/27723']
4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate(1-)
CHEBI:58909		consumes

4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735
  • RHEA:27735

    Source assertion: RHEA:27735 assigns CHEBI:58909 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27735']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27734_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27734_compound_5985']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5985)
water
CHEBI:15377		consumes

4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735
  • RHEA:27735

    Source assertion: RHEA:27735 assigns CHEBI:15377 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27735']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27734_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27734_compound_1283']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_1283)
4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735		produces

4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate zwitterion
CHEBI:60463
  • RHEA:27735

    Source assertion: RHEA:27735 assigns CHEBI:60463 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27735']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27734_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27734_compound_6257']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6257)
4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735		produces

formate
CHEBI:15740
  • RHEA:27735

    Source assertion: RHEA:27735 assigns CHEBI:15740 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27735']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27734_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27734_compound_3001']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3001)
4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735		part_of

Native 22.5 marks this step hypothetical; later experiments support the transformation. E. coli gene-disruption evidence and purified Salmonella enzyme evidence are distinguished.

MetaCyc:PWY0-1338
  • MetaCyc:PWY0-1338

    Source assertion: The native pathway explicitly includes RXN0-5409 in its six-reaction list.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-list/Reaction[@frameid="RXN0-5409"]
  • MetaCyc:RXN0-5409

    Source assertion: The native reaction carries the Rhea cross-reference 27735.

    Source location/ptools-xml/Reaction[@frameid="RXN0-5409"]/dblink[dblink-db="RHEA"]/dblink-oid
  • RHEA:27735

    Source assertion: Rhea master 27734 links directed reaction 27735; the selected orientation is left_to_right.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27734']/rh:directionalReaction[@rdf:resource='http://rdf.rhea-db.org/27735']
  • PMID:37782650

    Source assertion: Deleting arnD in the E. coli pmrAc background accumulates C55P-Ara4FN; purified Salmonella ArnD converts the substrate to C55P-Ara4N in vitro.

    Source locationPMC10914315, Results, P21 and P28; Figures 1D and 5A
4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate zwitterion
CHEBI:60463		consumes

2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372
  • RHEA:35372

    Source assertion: RHEA:35372 assigns CHEBI:60463 to its substrates with coefficient 2.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/35372']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/35371_L']/rh:contains2[@rdf:resource='http://rdf.rhea-db.org/Participant_35371_compound_6257']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6257)
  • PMID:11535605

    Source assertion: The purified E. coli donor lipid contains one phosphate and an alpha-linked L-Ara4N residue, as established by mass spectrometry and multidimensional NMR.

    Source location/resultList/result[id="11535605"]/abstractText
(Kdo)2-lipid A(6-) (E. coli)
CHEBI:58540		consumes

2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372
  • RHEA:35372

    Source assertion: RHEA:35372 assigns CHEBI:58540 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/35372']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/35371_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_35371_compound_5227']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5227)
2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372		produces

(beta-L-Ara4N)2-(KDO)2-lipid A(2-)
CHEBI:71399
  • RHEA:35372

    Source assertion: RHEA:35372 assigns CHEBI:71399 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/35372']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/35371_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_35371_compound_7725']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_7725)
2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372		produces

ditrans,polycis-undecaprenyl phosphate(2-)
CHEBI:60392
  • RHEA:35372

    Source assertion: RHEA:35372 assigns CHEBI:60392 to its products with coefficient 2.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/35372']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/35371_R']/rh:contains2[@rdf:resource='http://rdf.rhea-db.org/Participant_35371_compound_6255']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6255)
2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372		part_of

The current balanced equation represents two transfers to a Kdo-disaccharide-bearing lipid-A substrate. It does not impose double modification on every lipid-A molecule.

MetaCyc:PWY0-1338
  • MetaCyc:PWY0-1338

    Source assertion: The native pathway explicitly includes RXN0-2001 in its six-reaction list.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-list/Reaction[@frameid="RXN0-2001"]
  • MetaCyc:RXN0-2001

    Source assertion: The native reaction carries the Rhea cross-reference 35372.

    Source location/ptools-xml/Reaction[@frameid="RXN0-2001"]/dblink[dblink-db="RHEA"]/dblink-oid
  • RHEA:35372

    Source assertion: Rhea master 35371 links directed reaction 35372; the selected orientation is left_to_right.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/35371']/rh:directionalReaction[@rdf:resource='http://rdf.rhea-db.org/35372']
Bifunctional polymyxin resistance protein ArnA
UniProtKB:P77398		part_of

The named native hexamer represents the experimentally characterized assembly, not an exclusive oligomeric state or a claim that isolated domains are inactive.

UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
MetaCyc:CPLX0-7718
  • MetaCyc:CPLX0-7718

    Source assertion: The native complex contains six G7168-MONOMER subunits.

    Source location/ptools-xml/Protein[@frameid="CPLX0-7718"]/component/Protein; component/coefficient
  • UniProtKB:P77398

    Source assertion: SUBUNIT annotates a homohexamer, a dimer of trimers, with ECO:0000269 evidence from PMID15809294 and PMID15939024.

    Source location/comments/7/texts/0
  • PMID:15939024

    Source assertion: The full-length E. coli structure is a hexamer assembled as a dimer of trimers; crystal forms independently contain the same hexameric unit.

    Source locationPMC2997725, Results and Discussion, P8 and P10; Figure 2
  • PMID:31344437

    Source assertion: The inspected abstract reports both hexameric and tetrameric ArnA cryo-EM architectures and proposes an oligomeric equilibrium.

    Source location/resultList/result[id="31344437"]/abstractText
UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
MetaCyc:CPLX0-7718		catalyzes

NAD+ is a consumed and reduced substrate, not a permanently bound cofactor; ATP used in the crystal structure is a NAD+ mimic.

UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703
  • MetaCyc:CPLX0-7718

    Source assertion: The native ArnA complex catalyzes the enzyme reaction linked to RXN0-1861.

    Source location/ptools-xml/Protein[@frameid="CPLX0-7718"]/catalyzes/Enzymatic-Reaction/reaction/Reaction[@frameid="RXN0-1861"]
  • UniProtKB:P77398

    Source assertion: CATALYTIC ACTIVITY assigns NAD-dependent UDP-glucuronate oxidative decarboxylation (RHEA:24702; ECO:0000269), with physiological direction 24703.

    Source location/comments/1/reaction; /comments/1/physiologicalReactions/0
  • PMID:15807526

    Source assertion: Purified ArnA C-terminal domain converts UDP-glucuronate with NAD+ to the UDP-ketopentose used in the coupled ArnB reaction.

    Source locationPMC2583347, Materials and Methods, Thin-Layer Chromatography Assays, P14
  • PMID:15939024

    Source assertion: ATP is a structural mimic in the crystal; NAD+ binds, is reduced and is released as NADH as a true substrate.

    Source locationPMC2997725, P17 and P29
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
UniProtKB:P77690		enables

Biosynthetic flux selects the Rhea right-to-left direction of a reversible aminotransferase. The functional gene-product role does not assert monomer sufficiency; the E. coli dimer annotation is by similarity.

UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712
  • UniProtKB:P77690

    Source assertion: FUNCTION assigns production of UDP-aminoarabinose, and CATALYTIC ACTIVITY cites the reversible RHEA:24710 equation (ECO:0000269; PMID12704196).

    Source location/comments/0/texts/0; /comments/1/reaction
  • PMID:12704196

    Source assertion: Purified E. coli ArnB reversibly transfers the glutamate amino group to the UDP-ketopentose; NMR confirms the product, and the equilibrium constant toward UDP-aminoarabinose is about 0.1.

    Source location/resultList/result[id="12704196"]/abstractText
  • UniProtKB:P77690

    Source assertion: The homodimer SUBUNIT annotation is transferred by similarity from Salmonella Q8ZNF3 (ECO:0000250).

    Source location/comments/5/texts/0
UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronate dehydrogenase
MetaCyc:CPLX0-7718		catalyzes

Folate is the formyl-donating substrate. Active isolated domains do not establish that a hexamer is mandatory for either chemistry.

UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707
  • MetaCyc:CPLX0-7718

    Source assertion: The native ArnA complex catalyzes the enzyme reaction linked to RXN0-1862.

    Source location/ptools-xml/Protein[@frameid="CPLX0-7718"]/catalyzes/Enzymatic-Reaction/reaction/Reaction[@frameid="RXN0-1862"]
  • UniProtKB:P77398

    Source assertion: CATALYTIC ACTIVITY assigns formyl transfer from (6R)-10-formyltetrahydrofolate to UDP-aminoarabinose (RHEA:24706; ECO:0000269); physiological direction is 24707.

    Source location/comments/2/reaction; /comments/2/physiologicalReactions/0
  • PMID:15807526

    Source assertion: The isolated E. coli N-terminal domain retains transformylation activity; assays add N10-formyltetrahydrofolate to the UDP-aminoarabinose substrate.

    Source locationPMC2583347, Materials and Methods P14-P16; Results and Discussion P17-P19
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
UniProtKB:P77757		enables

Functional E. coli ArnC role. The later Salmonella tetramer structure and Mn-containing assays are not evidence for a fixed E. coli oligomer or its physiological metal.

UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723
  • UniProtKB:P77757

    Source assertion: CATALYTIC ACTIVITY assigns transfer of formamidoarabinose from UDP to undecaprenyl phosphate (RHEA:27722; ECO:0000269; PMID15695810).

    Source location/comments/1/reaction
  • PMID:15695810

    Source assertion: Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl-phosphate-linked form by ArnC.

    Source location/resultList/result[id="15695810"]/abstractText
  • MetaCyc:G7167-MONOMER

    Source assertion: The native comment distinguishes ArnC utilization of UDP-L-Ara4FN from failure to utilize unformylated UDP-L-Ara4N.

    Source location/ptools-xml/Protein[@frameid="G7167-MONOMER"]/comment
  • PMID:39865303

    Source assertion: The cryo-EM study uses Salmonella Typhimurium ArnC and observes apo and UDP-bound tetramers; this is not direct evidence for E. coli quaternary structure.

    Source locationPMC11761694, sections 2.1 (pro70037-sec-0003), 3.2 (pro70037-sec-0008) and 3.3 (pro70037-sec-0009)
  • PMID:37782650

    Source assertion: Substrate synthesis uses purified Salmonella ArnC in a reaction mixture containing MnCl2.

    Source locationPMC10914315, Materials and Methods P19
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
UniProtKB:P76472		enables

E. coli activity assignment is supported by genetics plus the reviewed annotation and separately scoped Salmonella biochemistry. No E. coli physiological metal or fixed assembly is asserted.

4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735
  • UniProtKB:P76472

    Source assertion: FUNCTION still labels deformylation probable (ECO:0000305); CATALYTIC ACTIVITY assigns RHEA:27734 with HAMAP and older PMID15695810 annotations.

    Source location/comments/0/texts/0; /comments/1/reaction
  • PMID:37782650

    Source assertion: E. coli K-12 pmrAc strain MST100 lacking arnD accumulates the formylated C55P-Ara4FN intermediate, supporting the cellular ArnD role.

    Source locationPMC10914315, Materials and Methods P10; Results P21; Figure 1D
  • PMID:37782650

    Source assertion: Purified Salmonella Typhimurium ArnD deformylates the C55 donor; EDTA inhibition and Mn2+/Co2+ restoration or stimulation establish metal dependence in those assays.

    Source locationPMC10914315, Results P28-P30; Figure 5A
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
UniProtKB:P76473		enables

Functional E. coli transferase role with native Kdo2-lipid-A substrate scope. The terminal equation is a two-transfer net reaction; the one-transfer lipid-IVA assay is an alternative substrate reaction, not this equation.

2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372
  • MetaCyc:G7170-MONOMER

    Source assertion: The native E. coli ArnT protein links its catalyzed enzyme reaction to RXN0-2001; its comment states that the Salmonella enzyme was studied more extensively.

    Source location/ptools-xml/Protein[@frameid="G7170-MONOMER"]/catalyzes/Enzymatic-Reaction/reaction; comment
  • UniProtKB:P76473

    Source assertion: FUNCTION assigns L-Ara4N transfer from the lipid-linked donor to lipid A (ECO:0000269; PMID11535604). Its catalytic text specifically describes the lipid-IVA alternative.

    Source location/comments/0/texts/0; /comments/1/reaction
  • PMID:11535604

    Source assertion: The study reports two L-Ara4N additions to lipid-A precursors containing a Kdo disaccharide, but only one addition to lipid IVA lacking Kdo; ArnT homologs were assigned in E. coli and Salmonella.

    Source location/resultList/result[id="11535604"]/abstractText
  • PMID:17928292

    Source assertion: Deletion of arnT in the E. coli pmrAc background abolishes lipid-A modification without the decreased donor accessibility observed for arnE/arnF mutants.

    Source locationPMC2613183, Results, ArnT Is Not Involved in the Transport of Undecaprenyl Phosphate-alpha-L-Ara4N, P36
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
UniProtKB:P77690		has_cofactor

pyridoxal 5'-phosphate(2-)
CHEBI:597326
  • UniProtKB:P77690

    Source assertion: The COFACTOR field identifies pyridoxal 5-prime-phosphate.

    Source location/comments/2/cofactors/0
  • PMID:12704196

    Source assertion: Purified E. coli ArnB contains pyridoxal phosphate detected spectrophotometrically; excess glutamate converts it to the pyridoxamine form.

    Source location/resultList/result[id="12704196"]/abstractText
Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE
UniProtKB:Q47377		enables

Transport-associated pathway role jointly requiring ArnE and ArnF in the studied mutant background; neither edge asserts individual sufficiency, an established physical heterodimer, or direct catalysis of a glycosyltransfer reaction.

MetaCyc:PWY0-1338
  • UniProtKB:Q47377

    Source assertion: FUNCTION assigns transfer of the aminoarabinose-phosphoundecaprenol donor from cytoplasmic to periplasmic side of the inner membrane (ECO:0000269; PMID17928292).

    Source location/comments/0/texts/0
  • PMID:17928292

    Source assertion: Deleting either arnE or arnF reduces donor accessibility to an impermeable probe and restores sensitivity in the pmrAc parent; heterodimer formation and energy coupling remain proposals.

    Source locationPMC2613183, Results P34-P36; Discussion P39-P40 and P45
Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF
UniProtKB:P76474		enables

Transport-associated pathway role jointly requiring ArnE and ArnF in the studied mutant background; neither edge asserts individual sufficiency, an established physical heterodimer, or direct catalysis of a glycosyltransfer reaction.

MetaCyc:PWY0-1338
  • UniProtKB:P76474

    Source assertion: FUNCTION assigns transfer of the aminoarabinose-phosphoundecaprenol donor from cytoplasmic to periplasmic side of the inner membrane (ECO:0000269; PMID17928292).

    Source location/comments/0/texts/0
  • PMID:17928292

    Source assertion: Deleting either arnE or arnF reduces donor accessibility to an impermeable probe and restores sensitivity in the pmrAc parent; heterodimer formation and energy coupling remain proposals.

    Source locationPMC2613183, Results P34-P36; Discussion P39-P40 and P45
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
UniProtKB:P77757		located_in

Inner membrane mapped to the plasma-membrane cellular component; this does not locate the whole pathway in one compartment.

plasma membrane
GO:0005886
  • UniProtKB:P77757

    Source assertion: SUBCELLULAR LOCATION annotates a multipass cell-inner-membrane protein. This field has no explicit experimental evidence code.

    Source location/comments/4/subcellularLocations/0
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
UniProtKB:P76473		located_in

Inner membrane mapped to the plasma-membrane cellular component; this does not locate the whole pathway in one compartment.

plasma membrane
GO:0005886
  • UniProtKB:P76473

    Source assertion: SUBCELLULAR LOCATION annotates a multipass cell-inner-membrane protein. The location evidence is ECO:0000269, PMID15919996.

    Source location/comments/3/subcellularLocations/0
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
UniProtKB:P77690		located_in

cytosol
GO:0005829
  • PMID:12704196

    Source assertion: The abstract identifies ArnB as a cytoplasmic protein purified from an E. coli overproducing strain.

    Source location/resultList/result[id="12704196"]/abstractText
UDP-alpha-D-glucuronate + NAD(+) => UDP-beta-L-threo-pentopyranos-4-ulose + CO2 + NADH
RHEA:24703		provides_input_for

The shared chemical class is CHEBI:58710.

UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712
  • MetaCyc:PWY0-1338

    Source assertion: The pathway orders RXN0-1861 before RXN0-1863.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-ordering[Reaction/@frameid="RXN0-1863"]/predecessor-reactions/Reaction[@frameid="RXN0-1861"]
  • RHEA:24703

    Source assertion: RHEA:24703 assigns CHEBI:58710 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24703']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24702_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24702_compound_5229']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5229)
  • RHEA:24712

    Source assertion: RHEA:24712 assigns CHEBI:58710 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24712']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24710_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24710_compound_5229']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5229)
UDP-beta-L-threo-pentopyranos-4-ulose + L-glutamate => UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
RHEA:24712		provides_input_for

The shared chemical class is CHEBI:58708.

UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707
  • MetaCyc:PWY0-1338

    Source assertion: The pathway orders RXN0-1863 before RXN0-1862.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-ordering[Reaction/@frameid="RXN0-1862"]/predecessor-reactions/Reaction[@frameid="RXN0-1863"]
  • RHEA:24712

    Source assertion: RHEA:24712 assigns CHEBI:58708 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24712']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24710_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24710_compound_5232']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5232)
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:58708 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_5232']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5232)
UDP-4-amino-4-deoxy-beta-L-arabinose + (6R)-10-formyltetrahydrofolate => UDP-4-deoxy-4-formamido-beta-L-arabinose + (6S)-5,6,7,8-tetrahydrofolate + H(+)
RHEA:24707		provides_input_for

The shared chemical class is CHEBI:58709.

UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723
  • MetaCyc:PWY0-1338

    Source assertion: The pathway orders RXN0-1862 before RXN0-3521.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-ordering[Reaction/@frameid="RXN0-3521"]/predecessor-reactions/Reaction[@frameid="RXN0-1862"]
  • RHEA:24707

    Source assertion: RHEA:24707 assigns CHEBI:58709 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/24707']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/24706_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_24706_compound_5231']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5231)
  • RHEA:27723

    Source assertion: RHEA:27723 assigns CHEBI:58709 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27723']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27722_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27722_compound_5231']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5231)
UDP-4-deoxy-4-formamido-beta-L-arabinose + di-trans,octa-cis-undecaprenyl phosphate => 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP
RHEA:27723		provides_input_for

The shared chemical class is CHEBI:58909.

4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735
  • MetaCyc:PWY0-1338

    Source assertion: The pathway orders RXN0-3521 before RXN0-5409.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-ordering[Reaction/@frameid="RXN0-5409"]/predecessor-reactions/Reaction[@frameid="RXN0-3521"]
  • RHEA:27723

    Source assertion: RHEA:27723 assigns CHEBI:58909 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27723']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27722_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27722_compound_5985']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5985)
  • RHEA:27735

    Source assertion: RHEA:27735 assigns CHEBI:58909 to its substrates with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27735']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27734_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27734_compound_5985']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_5985)
4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O => 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate
RHEA:27735		provides_input_for

The shared chemical class is CHEBI:60463. Donor transport by ArnE/ArnF is required between formation on the cytoplasmic side and ArnT utilization on the periplasmic side; this class-level edge is not direct substrate channeling.

2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A (E. coli) => (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate
RHEA:35372
  • MetaCyc:PWY0-1338

    Source assertion: The pathway orders RXN0-5409 before RXN0-2001.

    Source location/ptools-xml/Pathway[@frameid="PWY0-1338"]/reaction-ordering[Reaction/@frameid="RXN0-2001"]/predecessor-reactions/Reaction[@frameid="RXN0-5409"]
  • RHEA:27735

    Source assertion: RHEA:27735 assigns CHEBI:60463 to its products with coefficient 1.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/27735']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/27734_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_27734_compound_6257']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6257)
  • RHEA:35372

    Source assertion: RHEA:35372 assigns CHEBI:60463 to its substrates with coefficient 2.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/35372']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/35371_L']/rh:contains2[@rdf:resource='http://rdf.rhea-db.org/Participant_35371_compound_6257']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6257)
  • PMID:17928292

    Source assertion: The donor formed on the cytoplasmic side must reach the periplasmic face for ArnT use; deletion and labeling data implicate both ArnE and ArnF.

    Source locationPMC2613183, P7-P8, Results P34-P36; Discussion P39-P40

References

Curation history