allantoin degradation IV (anaerobic)

MetaCyc:PWY0-41

The Escherichia coli K-12 MG1655 anaerobic route converts S-allantoin through allantoate, S-ureidoglycine, S-ureidoglycolate and oxalurate to oxamate, with carbamoyl phosphate supporting ATP formation by AllK and subsequent spontaneous carbamate breakdown. The formal native endpoint is CO2, not a claim that dissolved inorganic carbon occurs exclusively as CO2. AllB, AllC and AllD have independently identified homomeric assemblies. AllF, AllG and AllH jointly supply OXTCase function; their enables edges preserve component roles without claiming individual sufficiency, a resolved whole-complex stoichiometry, or a formal AND relation. The Mg2+ context node refers to whole-OXTCase assay dependence and AllK assay conditions, not subunit-specific binding. The native mirror predates the 2024 AllFGH assignment and carries a stale AllC Rhea link; current protein and primary evidence resolve those limits. AllD uses NAD+, and alternative metal preparations are qualified at their edges. The separate glyoxylate branch, urea-producing yeast routes, transport, regulation, NADP substitution, bicarbonate hydration, and duplicate combined kinase/decomposition nets are outside this record.

Pathway type

allantoin degradation

Organism scope

Escherichia coli str. K-12 substr. MG1655 NCBITaxon:511145

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Pathway network

42 nodes · 61 asserted directed edges

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Dashed arrow: membership, location or cofactor relation

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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Escherichia coli str. K-12 substr. MG1655 `NCBITaxon:511145`	taxon
(S)-(+)-allantoin `CHEBI:15678`	small molecule
water `CHEBI:15377`	small molecule
allantoate `CHEBI:17536`	small molecule
hydron `CHEBI:15378`	small molecule
(S)-2-ureidoglycine zwitterion `CHEBI:59947`	small molecule
ammonium `CHEBI:28938`	small molecule
carbon dioxide `CHEBI:16526`	small molecule
(-)-ureidoglycolate `CHEBI:57296`	small molecule
NAD(1-) `CHEBI:57540`	small molecule
oxalurate `CHEBI:57824`	small molecule
NADH(2-) `CHEBI:57945`	small molecule
hydrogenphosphate `CHEBI:43474`	small molecule
oxamate `CHEBI:58363`	small molecule
carbamoyl phosphate(2-) `CHEBI:58228`	small molecule
ADP(3-) `CHEBI:456216`	small molecule
carbamate `CHEBI:13941`	small molecule
ATP(4-) `CHEBI:30616`	small molecule
zinc(2+) `CHEBI:29105`	cofactor
nickel(2+) `CHEBI:49786`	cofactor
cobalt(2+) `CHEBI:48828`	cofactor
manganese(2+) `CHEBI:29035`	cofactor
magnesium(2+) `CHEBI:18420`	cofactor
Allantoinase `UniProtKB:P77671`	protein
Allantoate amidohydrolase `UniProtKB:P77425`	protein
(S)-ureidoglycine aminohydrolase `UniProtKB:P75713`	protein
Ureidoglycolate dehydrogenase (NAD(+)) `UniProtKB:P77555`	protein
Oxamate carbamoyltransferase subunit AllF `UniProtKB:Q47208`	protein
Oxamate carbamoyltransferase subunit AllG `UniProtKB:P77129`	protein
Oxamate carbamoyltransferase subunit AllH `UniProtKB:P0AAS5`	protein
Carbamate kinase `UniProtKB:P37306`	protein
allantoinase `MetaCyc:CPLX-64`	complex
allantoate amidohydrolase `MetaCyc:CPLX-7524`	complex
ureidoglycolate dehydrogenase `MetaCyc:CPLX0-7993`	complex
cytoplasm `GO:0005737`	cellular component
(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	molecular activity	left to right
allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	molecular activity	left to right
(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	molecular activity	left to right
(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	molecular activity	left to right
N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	molecular activity	right to left
carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	molecular activity	right to left
carbamate + 2 H(+) => NH4(+) + CO2 `RHEA:15650`	reaction	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
(S)-(+)-allantoin `CHEBI:15678`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	RHEA:17029 Source assertion: RHEA:17030 substrates contain CHEBI:15678 with coefficient 1. Source location `http://rdf.rhea-db.org/17030 rh:substrates; http://rdf.rhea-db.org/17029_L rh:contains1 http://rdf.rhea-db.org/Participant_17029_compound_2545; rh:compound/rh:accession`
water `CHEBI:15377`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	RHEA:17029 Source assertion: RHEA:17030 substrates contain CHEBI:15377 with coefficient 1. Source location `http://rdf.rhea-db.org/17030 rh:substrates; http://rdf.rhea-db.org/17029_L rh:contains1 http://rdf.rhea-db.org/Participant_17029_compound_1283; rh:compound/rh:accession`
(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	allantoate `CHEBI:17536`	RHEA:17029 Source assertion: RHEA:17030 products contain CHEBI:17536 with coefficient 1. Source location `http://rdf.rhea-db.org/17030 rh:products; http://rdf.rhea-db.org/17029_R rh:contains1 http://rdf.rhea-db.org/Participant_17029_compound_4604; rh:compound/rh:accession`
(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	hydron `CHEBI:15378`	RHEA:17029 Source assertion: RHEA:17030 products contain CHEBI:15378 with coefficient 1. Source location `http://rdf.rhea-db.org/17030 rh:products; http://rdf.rhea-db.org/17029_R rh:contains1 http://rdf.rhea-db.org/Participant_17029_compound_3249; rh:compound/rh:accession`
allantoate `CHEBI:17536`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	RHEA:27485 Source assertion: RHEA:27486 substrates contain CHEBI:17536 with coefficient 1. Source location `http://rdf.rhea-db.org/27486 rh:substrates; http://rdf.rhea-db.org/27485_L rh:contains1 http://rdf.rhea-db.org/Participant_27485_compound_4604; rh:compound/rh:accession`
water `CHEBI:15377`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	RHEA:27485 Source assertion: RHEA:27486 substrates contain CHEBI:15377 with coefficient 1. Source location `http://rdf.rhea-db.org/27486 rh:substrates; http://rdf.rhea-db.org/27485_L rh:contains1 http://rdf.rhea-db.org/Participant_27485_compound_1283; rh:compound/rh:accession`
hydron `CHEBI:15378`	consumes Coefficient 2 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	RHEA:27485 Source assertion: RHEA:27486 substrates contain CHEBI:15378 with coefficient 2. Source location `http://rdf.rhea-db.org/27486 rh:substrates; http://rdf.rhea-db.org/27485_L rh:contains2 http://rdf.rhea-db.org/Participant_27485_compound_3249; rh:compound/rh:accession`
allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-2-ureidoglycine zwitterion `CHEBI:59947`	RHEA:27485 Source assertion: RHEA:27486 products contain CHEBI:59947 with coefficient 1. Source location `http://rdf.rhea-db.org/27486 rh:products; http://rdf.rhea-db.org/27485_R rh:contains1 http://rdf.rhea-db.org/Participant_27485_compound_6148; rh:compound/rh:accession`
allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	ammonium `CHEBI:28938`	RHEA:27485 Source assertion: RHEA:27486 products contain CHEBI:28938 with coefficient 1. Source location `http://rdf.rhea-db.org/27486 rh:products; http://rdf.rhea-db.org/27485_R rh:contains1 http://rdf.rhea-db.org/Participant_27485_compound_1012; rh:compound/rh:accession`
allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbon dioxide `CHEBI:16526`	RHEA:27485 Source assertion: RHEA:27486 products contain CHEBI:16526 with coefficient 1. Source location `http://rdf.rhea-db.org/27486 rh:products; http://rdf.rhea-db.org/27485_R rh:contains1 http://rdf.rhea-db.org/Participant_27485_compound_4391; rh:compound/rh:accession`
(S)-2-ureidoglycine zwitterion `CHEBI:59947`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	RHEA:25241 Source assertion: RHEA:25242 substrates contain CHEBI:59947 with coefficient 1. Source location `http://rdf.rhea-db.org/25242 rh:substrates; http://rdf.rhea-db.org/25241_L rh:contains1 http://rdf.rhea-db.org/Participant_25241_compound_6148; rh:compound/rh:accession`
water `CHEBI:15377`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	RHEA:25241 Source assertion: RHEA:25242 substrates contain CHEBI:15377 with coefficient 1. Source location `http://rdf.rhea-db.org/25242 rh:substrates; http://rdf.rhea-db.org/25241_L rh:contains1 http://rdf.rhea-db.org/Participant_25241_compound_1283; rh:compound/rh:accession`
(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(-)-ureidoglycolate `CHEBI:57296`	RHEA:25241 Source assertion: RHEA:25242 products contain CHEBI:57296 with coefficient 1. Source location `http://rdf.rhea-db.org/25242 rh:products; http://rdf.rhea-db.org/25241_R rh:contains1 http://rdf.rhea-db.org/Participant_25241_compound_4140; rh:compound/rh:accession`
(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	ammonium `CHEBI:28938`	RHEA:25241 Source assertion: RHEA:25242 products contain CHEBI:28938 with coefficient 1. Source location `http://rdf.rhea-db.org/25242 rh:products; http://rdf.rhea-db.org/25241_R rh:contains1 http://rdf.rhea-db.org/Participant_25241_compound_1012; rh:compound/rh:accession`
(-)-ureidoglycolate `CHEBI:57296`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	RHEA:15329 Source assertion: RHEA:15330 substrates contain CHEBI:57296 with coefficient 1. Source location `http://rdf.rhea-db.org/15330 rh:substrates; http://rdf.rhea-db.org/15329_L rh:contains1 http://rdf.rhea-db.org/Participant_15329_compound_4140; rh:compound/rh:accession`
NAD(1-) `CHEBI:57540`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	RHEA:15329 Source assertion: RHEA:15330 substrates contain CHEBI:57540 with coefficient 1. Source location `http://rdf.rhea-db.org/15330 rh:substrates; http://rdf.rhea-db.org/15329_L rh:contains1 http://rdf.rhea-db.org/Participant_15329_compound_3484; rh:compound/rh:accession`
(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	oxalurate `CHEBI:57824`	RHEA:15329 Source assertion: RHEA:15330 products contain CHEBI:57824 with coefficient 1. Source location `http://rdf.rhea-db.org/15330 rh:products; http://rdf.rhea-db.org/15329_R rh:contains1 http://rdf.rhea-db.org/Participant_15329_compound_1605; rh:compound/rh:accession`
(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	NADH(2-) `CHEBI:57945`	RHEA:15329 Source assertion: RHEA:15330 products contain CHEBI:57945 with coefficient 1. Source location `http://rdf.rhea-db.org/15330 rh:products; http://rdf.rhea-db.org/15329_R rh:contains1 http://rdf.rhea-db.org/Participant_15329_compound_1650; rh:compound/rh:accession`
(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	hydron `CHEBI:15378`	RHEA:15329 Source assertion: RHEA:15330 products contain CHEBI:15378 with coefficient 1. Source location `http://rdf.rhea-db.org/15330 rh:products; http://rdf.rhea-db.org/15329_R rh:contains1 http://rdf.rhea-db.org/Participant_15329_compound_3249; rh:compound/rh:accession`
oxalurate `CHEBI:57824`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	RHEA:22984 Source assertion: RHEA:22986 substrates contain CHEBI:57824 with coefficient 1. Source location `http://rdf.rhea-db.org/22986 rh:substrates; http://rdf.rhea-db.org/22984_R rh:contains1 http://rdf.rhea-db.org/Participant_22984_compound_1605; rh:compound/rh:accession`
hydrogenphosphate `CHEBI:43474`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	RHEA:22984 Source assertion: RHEA:22986 substrates contain CHEBI:43474 with coefficient 1. Source location `http://rdf.rhea-db.org/22986 rh:substrates; http://rdf.rhea-db.org/22984_R rh:contains1 http://rdf.rhea-db.org/Participant_22984_compound_5518; rh:compound/rh:accession`
N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	oxamate `CHEBI:58363`	RHEA:22984 Source assertion: RHEA:22986 products contain CHEBI:58363 with coefficient 1. Source location `http://rdf.rhea-db.org/22986 rh:products; http://rdf.rhea-db.org/22984_L rh:contains1 http://rdf.rhea-db.org/Participant_22984_compound_1815; rh:compound/rh:accession`
N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbamoyl phosphate(2-) `CHEBI:58228`	RHEA:22984 Source assertion: RHEA:22986 products contain CHEBI:58228 with coefficient 1. Source location `http://rdf.rhea-db.org/22986 rh:products; http://rdf.rhea-db.org/22984_L rh:contains1 http://rdf.rhea-db.org/Participant_22984_compound_4600; rh:compound/rh:accession`
carbamoyl phosphate(2-) `CHEBI:58228`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	RHEA:30755 Source assertion: RHEA:30757 substrates contain CHEBI:58228 with coefficient 1. Source location `http://rdf.rhea-db.org/30757 rh:substrates; http://rdf.rhea-db.org/30755_R rh:contains1 http://rdf.rhea-db.org/Participant_30755_compound_4600; rh:compound/rh:accession`
ADP(3-) `CHEBI:456216`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	RHEA:30755 Source assertion: RHEA:30757 substrates contain CHEBI:456216 with coefficient 1. Source location `http://rdf.rhea-db.org/30757 rh:substrates; http://rdf.rhea-db.org/30755_R rh:contains1 http://rdf.rhea-db.org/Participant_30755_compound_2710; rh:compound/rh:accession`
carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbamate `CHEBI:13941`	RHEA:30755 Source assertion: RHEA:30757 products contain CHEBI:13941 with coefficient 1. Source location `http://rdf.rhea-db.org/30757 rh:products; http://rdf.rhea-db.org/30755_L rh:contains1 http://rdf.rhea-db.org/Participant_30755_compound_4239; rh:compound/rh:accession`
carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	ATP(4-) `CHEBI:30616`	RHEA:30755 Source assertion: RHEA:30757 products contain CHEBI:30616 with coefficient 1. Source location `http://rdf.rhea-db.org/30757 rh:products; http://rdf.rhea-db.org/30755_L rh:contains1 http://rdf.rhea-db.org/Participant_30755_compound_6372; rh:compound/rh:accession`
carbamate `CHEBI:13941`	consumes Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbamate + 2 H(+) => NH4(+) + CO2 `RHEA:15650`	RHEA:15649 Source assertion: RHEA:15650 substrates contain CHEBI:13941 with coefficient 1. Source location `http://rdf.rhea-db.org/15650 rh:substrates; http://rdf.rhea-db.org/15649_L rh:contains1 http://rdf.rhea-db.org/Participant_15649_compound_4239; rh:compound/rh:accession`
hydron `CHEBI:15378`	consumes Coefficient 2 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbamate + 2 H(+) => NH4(+) + CO2 `RHEA:15650`	RHEA:15649 Source assertion: RHEA:15650 substrates contain CHEBI:15378 with coefficient 2. Source location `http://rdf.rhea-db.org/15650 rh:substrates; http://rdf.rhea-db.org/15649_L rh:contains2 http://rdf.rhea-db.org/Participant_15649_compound_3249; rh:compound/rh:accession`
carbamate + 2 H(+) => NH4(+) + CO2 `RHEA:15650`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	ammonium `CHEBI:28938`	RHEA:15649 Source assertion: RHEA:15650 products contain CHEBI:28938 with coefficient 1. Source location `http://rdf.rhea-db.org/15650 rh:products; http://rdf.rhea-db.org/15649_R rh:contains1 http://rdf.rhea-db.org/Participant_15649_compound_1012; rh:compound/rh:accession`
carbamate + 2 H(+) => NH4(+) + CO2 `RHEA:15650`	produces Coefficient 1 in the selected directed Rhea equation; formal stereochemistry and charge are retained.	carbon dioxide `CHEBI:16526`	RHEA:15649 Source assertion: RHEA:15650 products contain CHEBI:16526 with coefficient 1. Source location `http://rdf.rhea-db.org/15650 rh:products; http://rdf.rhea-db.org/15649_R rh:contains1 http://rdf.rhea-db.org/Participant_15649_compound_4391; rh:compound/rh:accession`
(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	part_of Native pathway reaction, with the directed current Rhea chemistry independently resolved.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 contains the ammonia-producing upstream subpathway PWY-5698. Source location `Pathway[@frameid="PWY0-41"]/sub-pathways; reaction-list` MetaCyc:PWY-5698 Source assertion: PWY-5698 includes native reaction ALLANTOINASE-RXN. Source location `Pathway[@frameid="PWY-5698"]/reaction-list` MetaCyc:ALLANTOINASE-RXN Source assertion: The native reaction links to RHEA:17030; its participants agree with the selected physiological transformation. Source location `Reaction/left; Reaction/right; Reaction/dblink` RHEA:17029 Source assertion: RHEA:17029 has directional reaction RHEA:17030. Source location `http://rdf.rhea-db.org/17029 rh:directionalReaction`
allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	part_of Native pathway reaction, with the directed current Rhea chemistry independently resolved. The obsolete native cross-reference is rejected rather than silently reused.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 contains the ammonia-producing upstream subpathway PWY-5698. Source location `Pathway[@frameid="PWY0-41"]/sub-pathways; reaction-list` MetaCyc:PWY-5698 Source assertion: PWY-5698 includes native reaction ALLANTOATE-DEIMINASE-RXN. Source location `Pathway[@frameid="PWY-5698"]/reaction-list` MetaCyc:ALLANTOATE-DEIMINASE-RXN Source assertion: Native sides produce S-ureidoglycine, ammonium and carbon dioxide from allantoate; the old Rhea13594 link is not accepted as the current mapping. Source location `Reaction/left; Reaction/right; Reaction/dblink` UniProtKB:P77425 Source assertion: Current AllC catalytic annotation identifies the ureidoglycine-producing reaction as RHEA:27485, supported by PMID:20038185. Evidence: ECO:0000269. Source location `comments[1].reaction.reactionCrossReferences; evidences` RHEA:27485 Source assertion: RHEA:27485 has directional reaction RHEA:27486. Source location `http://rdf.rhea-db.org/27485 rh:directionalReaction`
(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	part_of Native pathway reaction, with the directed current Rhea chemistry independently resolved.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 contains the ammonia-producing upstream subpathway PWY-5698. Source location `Pathway[@frameid="PWY0-41"]/sub-pathways; reaction-list` MetaCyc:PWY-5698 Source assertion: PWY-5698 includes native reaction URUR-RXN. Source location `Pathway[@frameid="PWY-5698"]/reaction-list` MetaCyc:URUR-RXN Source assertion: The native reaction links to RHEA:25242; its participants agree with the selected physiological transformation. Source location `Reaction/left; Reaction/right; Reaction/dblink` RHEA:25241 Source assertion: RHEA:25241 has directional reaction RHEA:25242. Source location `http://rdf.rhea-db.org/25241 rh:directionalReaction`
(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	part_of Native pathway reaction, with the directed current Rhea chemistry independently resolved.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 includes native reaction RXN0-7024. Source location `Pathway[@frameid="PWY0-41"]/reaction-list` MetaCyc:RXN0-7024 Source assertion: The native reaction links to RHEA:15330; its participants agree with the selected physiological transformation. Source location `Reaction/left; Reaction/right; Reaction/dblink` RHEA:15329 Source assertion: RHEA:15329 has directional reaction RHEA:15330. Source location `http://rdf.rhea-db.org/15329 rh:directionalReaction`
N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	part_of Native pathway reaction, with the directed current Rhea chemistry independently resolved. The mirror still marks the enzyme hypothetical; the 2024 AllFGH study supplies experimental support.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 includes native reaction OXAMATE-CARBAMOYLTRANSFERASE-RXN. Source location `Pathway[@frameid="PWY0-41"]/reaction-list` MetaCyc:OXAMATE-CARBAMOYLTRANSFERASE-RXN Source assertion: The native reaction links to RHEA:22986; its participants agree with the selected physiological transformation. Source location `Reaction/left; Reaction/right; Reaction/dblink` RHEA:22984 Source assertion: RHEA:22984 has directional reaction RHEA:22986. Source location `http://rdf.rhea-db.org/22984 rh:directionalReaction`
carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	part_of Native pathway reaction, with the directed current Rhea chemistry independently resolved.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 includes native reaction RXN-14196. Source location `Pathway[@frameid="PWY0-41"]/reaction-list` MetaCyc:RXN-14196 Source assertion: The native reaction links to RHEA:30758; its participants agree with the selected physiological transformation. Source location `Reaction/left; Reaction/right; Reaction/dblink` RHEA:30755 Source assertion: RHEA:30755 has directional reaction RHEA:30757; native cross-reference RHEA:30758 is its bidirectional reaction. Source location `http://rdf.rhea-db.org/30755 rh:directionalReaction; rh:bidirectionalReaction`
carbamate + 2 H(+) => NH4(+) + CO2 `RHEA:15650`	part_of Spontaneous carbamate decomposition with the native CO2 endpoint; no enzyme is assigned. The bicarbonate alternative and combined kinase net are excluded to avoid duplicate chemistry.	`MetaCyc:PWY0-41`	MetaCyc:PWY0-41 Source assertion: PWY0-41 includes native reaction RXN0-5222. Source location `Pathway[@frameid="PWY0-41"]/reaction-list` MetaCyc:RXN0-5222 Source assertion: The native reaction links to RHEA:15650; its participants agree with the selected physiological transformation. Source location `Reaction/left; Reaction/right; Reaction/dblink` RHEA:15649 Source assertion: RHEA:15649 has directional reaction RHEA:15650. Source location `http://rdf.rhea-db.org/15649 rh:directionalReaction` MetaCyc:RXN0-5222 Source assertion: RXN0-5222 is marked spontaneous and converts carbamate plus two protons to ammonium and carbon dioxide. Source location `Reaction/spontaneous; left; right; reaction-direction`
Allantoinase `UniProtKB:P77671`	part_of 4 identical P77671 subunits form this native assembly; the protein is not separately assigned isolated-subunit catalysis.	allantoinase `MetaCyc:CPLX-64`	MetaCyc:CPLX-64 Source assertion: The native complex contains 4 copies of its protein monomer. Source location `Protein/component/Protein; Protein/component/coefficient` UniProtKB:P77671 Source assertion: Homotetramer annotation supports the assembly; its BioCyc monomer cross-reference grounds the component identity. Evidence: ECO:0000269. Source location `comments[6] SUBUNIT; uniProtKBCrossReferences[database=BioCyc]` PMID:11092864 Source assertion: The experimentally characterized protein is tetrameric. Source location `Results, purification and native molecular-mass determination`
Allantoate amidohydrolase `UniProtKB:P77425`	part_of 2 identical P77425 subunits form this native assembly; the protein is not separately assigned isolated-subunit catalysis.	allantoate amidohydrolase `MetaCyc:CPLX-7524`	MetaCyc:CPLX-7524 Source assertion: The native complex contains 2 copies of its protein monomer. Source location `Protein/component/Protein; Protein/component/coefficient` UniProtKB:P77425 Source assertion: Homodimer annotation supports the assembly; its BioCyc monomer cross-reference grounds the component identity. Evidence: ECO:0000269. Source location `comments[6] SUBUNIT; uniProtKBCrossReferences[database=BioCyc]` PMID:17362992 Source assertion: The AllC structural study describes its dimerization domain. Source location `Abstract, dimerization domain and overall assembly`
Ureidoglycolate dehydrogenase (NAD(+)) `UniProtKB:P77555`	part_of 2 identical P77555 subunits form this native assembly; the protein is not separately assigned isolated-subunit catalysis.	ureidoglycolate dehydrogenase `MetaCyc:CPLX0-7993`	MetaCyc:CPLX0-7993 Source assertion: The native complex contains 2 copies of its protein monomer. Source location `Protein/component/Protein; Protein/component/coefficient` UniProtKB:P77555 Source assertion: Homodimer annotation supports the assembly; its BioCyc monomer cross-reference grounds the component identity. Evidence: ECO:0000269. Source location `comments[4] SUBUNIT; uniProtKBCrossReferences[database=BioCyc]` PMID:23284870 Source assertion: The experimentally characterized protein is dimeric. Source location `Results/Overall Structure (s2a), size-exclusion chromatography and dimer interface`
allantoinase `MetaCyc:CPLX-64`	catalyzes Purified E. coli AllB hydrolyzes allantoin; the native tetramer is used as the catalyst.	(S)-allantoin + H2O => allantoate + H(+) `RHEA:17030`	UniProtKB:P77671 Source assertion: Catalytic activity identifies RHEA:17029 for this experimentally characterized protein. Evidence: ECO:0000269. Source location `comments[1].reaction; evidences` PMID:11092864 Source assertion: Purified E. coli AllB hydrolyzes allantoin; the native tetramer is used as the catalyst. Source location `Results, allantoinase purification and activity` MetaCyc:CPLX-64 Source assertion: The native assembly is linked to the corresponding enzymatic reaction. Source location `Protein/catalyzes`
allantoate amidohydrolase `MetaCyc:CPLX-7524`	catalyzes AllC produces S-ureidoglycine; separate AllE activity is needed for subsequent ureidoglycolate formation.	allantoate + H2O + 2 H(+) => (S)-2-ureidoglycine + NH4(+) + CO2 `RHEA:27486`	UniProtKB:P77425 Source assertion: Catalytic activity identifies RHEA:27485 for this experimentally characterized protein. Evidence: ECO:0000269. Source location `comments[1].reaction; evidences` PMID:20038185 Source assertion: AllC produces S-ureidoglycine; separate AllE activity is needed for subsequent ureidoglycolate formation. Source location `Abstract, reassignment of two successive bacterial reactions` MetaCyc:CPLX-7524 Source assertion: The native assembly is linked to the corresponding enzymatic reaction. Source location `Protein/catalyzes`
ureidoglycolate dehydrogenase `MetaCyc:CPLX0-7993`	catalyzes AllD is an NAD-dependent ureidoglycolate dehydrogenase; the dimer is supported by structure and solution size exclusion.	(S)-ureidoglycolate + NAD(+) => N-carbamoyl-2-oxoglycine + NADH + H(+) `RHEA:15330`	UniProtKB:P77555 Source assertion: Catalytic activity identifies RHEA:15329 for this experimentally characterized protein. Evidence: ECO:0000269. Source location `comments[1].reaction; evidences` PMID:23284870 Source assertion: AllD is an NAD-dependent ureidoglycolate dehydrogenase; the dimer is supported by structure and solution size exclusion. Source location `Results s2a; Introduction, cofactor specificity; Figure S2` MetaCyc:CPLX0-7993 Source assertion: The native assembly is linked to the corresponding enzymatic reaction. Source location `Protein/catalyzes`
(S)-ureidoglycine aminohydrolase `UniProtKB:P75713`	catalyzes AllE catalyzes the second, distinct hydrolysis to S-ureidoglycolate. Current monomer assignment is curator inference, not an experimental oligomerization claim.	(S)-2-ureidoglycine + H2O => (S)-ureidoglycolate + NH4(+) `RHEA:25242`	UniProtKB:P75713 Source assertion: AllE catalytic activity is RHEA:25241 (experimental evidence PMID:19935661; curator inference PMID:20038185); SUBUNIT is monomer by curator inference. Source location `comments[1].reaction; comments[3] SUBUNIT` PMID:19935661 Source assertion: Ureidoglycine aminohydrolase catalyzes formation of ureidoglycolate in the characterized ureide-degradation system. Source location `Abstract` PMID:20038185 Source assertion: Bacterial AllE catalyzes the step after AllC produces S-ureidoglycine. Source location `Abstract`
Oxamate carbamoyltransferase subunit AllF `UniProtKB:Q47208`	enables Functional component of jointly required AllF/AllG/AllH oxamate carbamoyltransferase. No single-subunit sufficiency, resolved assembly stoichiometry, or formal graph AND gate is asserted. Purified reverse-direction assays used coexpressed protein and Mg2+; catabolic direction is supported by genetics and current annotation.	N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	UniProtKB:Q47208 Source assertion: AllF/G/H are the three OXTCase component types (ECO:0000269); physiological RHEA:22986 direction is curator inference (ECO:0000305) from PMID:38888336. Source location `comments[0] FUNCTION; comments[1].physiologicalReactions; comments[5] SUBUNIT` PMID:38888336 Source assertion: All three gene products jointly restore oxamate formation; coexpressed purified protein catalyzes the reverse oxamate-plus-carbamoyl-phosphate assay. Whole-assembly stoichiometry remains unresolved. Evidence: ECO:0000269. Source location `Results s2-1 to s2-5; Tables 1-3; Discussion s3` PMID:38888336 Source assertion: Mg2+ dependence was tested on the enzyme preparation; purified assays used 10 mM MgCl2. This does not assign a metal-binding site to an isolated subunit. Source location `Results s2-4, Figure 4C; Methods s4-5`
Oxamate carbamoyltransferase subunit AllG `UniProtKB:P77129`	enables Functional component of jointly required AllF/AllG/AllH oxamate carbamoyltransferase. No single-subunit sufficiency, resolved assembly stoichiometry, or formal graph AND gate is asserted. Purified reverse-direction assays used coexpressed protein and Mg2+; catabolic direction is supported by genetics and current annotation.	N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	UniProtKB:P77129 Source assertion: AllF/G/H are the three OXTCase component types (ECO:0000269); physiological RHEA:22986 direction is curator inference (ECO:0000305) from PMID:38888336. Source location `comments[0] FUNCTION; comments[1].physiologicalReactions; comments[5] SUBUNIT` PMID:38888336 Source assertion: All three gene products jointly restore oxamate formation; coexpressed purified protein catalyzes the reverse oxamate-plus-carbamoyl-phosphate assay. Whole-assembly stoichiometry remains unresolved. Evidence: ECO:0000269. Source location `Results s2-1 to s2-5; Tables 1-3; Discussion s3` PMID:38888336 Source assertion: Mg2+ dependence was tested on the enzyme preparation; purified assays used 10 mM MgCl2. This does not assign a metal-binding site to an isolated subunit. Source location `Results s2-4, Figure 4C; Methods s4-5`
Oxamate carbamoyltransferase subunit AllH `UniProtKB:P0AAS5`	enables Functional component of jointly required AllF/AllG/AllH oxamate carbamoyltransferase. No single-subunit sufficiency, resolved assembly stoichiometry, or formal graph AND gate is asserted. Purified reverse-direction assays used coexpressed protein and Mg2+; catabolic direction is supported by genetics and current annotation.	N-carbamoyl-2-oxoglycine + phosphate => oxamate + carbamoyl phosphate `RHEA:22986`	UniProtKB:P0AAS5 Source assertion: AllF/G/H are the three OXTCase component types (ECO:0000269); physiological RHEA:22986 direction is curator inference (ECO:0000305) from PMID:38888336. Source location `comments[0] FUNCTION; comments[1].physiologicalReactions; comments[5] SUBUNIT` PMID:38888336 Source assertion: All three gene products jointly restore oxamate formation; coexpressed purified protein catalyzes the reverse oxamate-plus-carbamoyl-phosphate assay. Whole-assembly stoichiometry remains unresolved. Evidence: ECO:0000269. Source location `Results s2-1 to s2-5; Tables 1-3; Discussion s3` PMID:38888336 Source assertion: Mg2+ dependence was tested on the enzyme preparation; purified assays used 10 mM MgCl2. This does not assign a metal-binding site to an isolated subunit. Source location `Results s2-4, Figure 4C; Methods s4-5`
Carbamate kinase `UniProtKB:P37306`	enables AllK (YbcF) supplies ATP-forming carbamate kinase activity; no unverified oligomeric state is imposed. The assay used 30 mM MgCl2 without establishing an isolated enzyme-metal binding requirement. Carbamate decomposition is represented separately.	carbamoyl phosphate + ADP => carbamate + ATP `RHEA:30757`	UniProtKB:P37306 Source assertion: The component kinase reaction RHEA:30755 and physiological direction RHEA:30757 have ECO:0000305 evidence from PMID:36384810; the combined bicarbonate net is a separate annotation. Evidence: ECO:0000305. Source location `comments[2].reaction; comments[2].physiologicalReactions` PMID:36384810 Source assertion: Purified YbcF generated ATP from carbamoyl phosphate and ADP; substrate-dependent kinetics establish catabolic carbamate kinase activity. Evidence: ECO:0000269. Source location `Results sec15, Figures 4-6; Methods, Carbamate Kinase Assay`
allantoinase `MetaCyc:CPLX-64`	has_cofactor AllB metal alternative supported by current annotation. Zinc, nickel, cobalt and manganese are not four simultaneous requirements; measured metal occupancy and stereoselectivity depend on preparation.	zinc(2+) `CHEBI:29105`	UniProtKB:P77671 Source assertion: AllB uses Zn2+ and can also use Ni2+, Co2+ or Mn2+; the annotation combines experimental and curator-inference evidence. Source location `comments[2] COFACTOR; cofactors; note` PMID:12486048 Source assertion: Metal-substituted E. coli allantoinase preparations differ in activity and substrate stereoselectivity; measured metal occupancy is preparation dependent. Source location `Abstract; Results, metal analyses and substrate specificity`
allantoinase `MetaCyc:CPLX-64`	has_cofactor AllB metal alternative supported by current annotation. Zinc, nickel, cobalt and manganese are not four simultaneous requirements; measured metal occupancy and stereoselectivity depend on preparation.	nickel(2+) `CHEBI:49786`	UniProtKB:P77671 Source assertion: AllB uses Zn2+ and can also use Ni2+, Co2+ or Mn2+; the annotation combines experimental and curator-inference evidence. Source location `comments[2] COFACTOR; cofactors; note` PMID:12486048 Source assertion: Metal-substituted E. coli allantoinase preparations differ in activity and substrate stereoselectivity; measured metal occupancy is preparation dependent. Source location `Abstract; Results, metal analyses and substrate specificity`
allantoinase `MetaCyc:CPLX-64`	has_cofactor AllB metal alternative supported by current annotation. Zinc, nickel, cobalt and manganese are not four simultaneous requirements; measured metal occupancy and stereoselectivity depend on preparation.	cobalt(2+) `CHEBI:48828`	UniProtKB:P77671 Source assertion: AllB uses Zn2+ and can also use Ni2+, Co2+ or Mn2+; the annotation combines experimental and curator-inference evidence. Source location `comments[2] COFACTOR; cofactors; note` PMID:12486048 Source assertion: Metal-substituted E. coli allantoinase preparations differ in activity and substrate stereoselectivity; measured metal occupancy is preparation dependent. Source location `Abstract; Results, metal analyses and substrate specificity`
allantoinase `MetaCyc:CPLX-64`	has_cofactor AllB metal alternative supported by current annotation. Zinc, nickel, cobalt and manganese are not four simultaneous requirements; measured metal occupancy and stereoselectivity depend on preparation.	manganese(2+) `CHEBI:29035`	UniProtKB:P77671 Source assertion: AllB uses Zn2+ and can also use Ni2+, Co2+ or Mn2+; the annotation combines experimental and curator-inference evidence. Source location `comments[2] COFACTOR; cofactors; note` PMID:12486048 Source assertion: Metal-substituted E. coli allantoinase preparations differ in activity and substrate stereoselectivity; measured metal occupancy is preparation dependent. Source location `Abstract; Results, metal analyses and substrate specificity`
allantoate amidohydrolase `MetaCyc:CPLX-7524`	has_cofactor The earlier AllC structure reports two Zn2+ ions per subunit; this bound-metal annotation does not establish zinc as the unique physiological metal.	zinc(2+) `CHEBI:29105`	UniProtKB:P77425 Source assertion: The earlier AllC structure reports two Zn2+ ions per subunit; this bound-metal annotation does not establish zinc as the unique physiological metal. Evidence: ECO:0000269. Source location `comments[2] COFACTOR; note` PMID:17362992 Source assertion: The study supports the binuclear zinc-containing AllC active center. Source location `Abstract`
allantoate amidohydrolase `MetaCyc:CPLX-7524`	has_cofactor AllC can bind Mn2+; subsequent functional work characterizes manganese-dependent chemistry. Metal selection is source- and preparation-dependent.	manganese(2+) `CHEBI:29035`	UniProtKB:P77425 Source assertion: AllC can bind Mn2+; subsequent functional work characterizes manganese-dependent chemistry. Metal selection is source- and preparation-dependent. Evidence: ECO:0000269. Source location `comments[2] COFACTOR; note` PMID:20038185 Source assertion: The study supports manganese-dependent activity in the bacterial AllC/AllE degradation sequence. Source location `Abstract`
(S)-ureidoglycine aminohydrolase `UniProtKB:P75713`	has_cofactor AllE uses manganese and can alternatively use cobalt; these are alternatives, not simultaneous requirements.	manganese(2+) `CHEBI:29035`	UniProtKB:P75713 Source assertion: AllE has Mn2+ as cofactor and can also use Co2+, with experimental evidence from PMID:20038185. Evidence: ECO:0000269. Source location `comments[2] COFACTOR; note`
(S)-ureidoglycine aminohydrolase `UniProtKB:P75713`	has_cofactor AllE uses manganese and can alternatively use cobalt; these are alternatives, not simultaneous requirements.	cobalt(2+) `CHEBI:48828`	UniProtKB:P75713 Source assertion: AllE has Mn2+ as cofactor and can also use Co2+, with experimental evidence from PMID:20038185. Evidence: ECO:0000269. Source location `comments[2] COFACTOR; note`
Allantoate amidohydrolase `UniProtKB:P77425`	located_in Protein-level cytoplasmic localization; the cited annotation evidence grade is retained and not extended to unannotated partners.	cytoplasm `GO:0005737`	UniProtKB:P77425 Source assertion: The protein is annotated in the cytoplasm (SL-0086). Evidence: ECO:0000305. Source location `comments[7] SUBCELLULAR LOCATION`
(S)-ureidoglycine aminohydrolase `UniProtKB:P75713`	located_in Protein-level cytoplasmic localization; the cited annotation evidence grade is retained and not extended to unannotated partners.	cytoplasm `GO:0005737`	UniProtKB:P75713 Source assertion: The protein is annotated in the cytoplasm (SL-0086). Evidence: ECO:0000269. Source location `comments[4] SUBCELLULAR LOCATION`
Ureidoglycolate dehydrogenase (NAD(+)) `UniProtKB:P77555`	located_in Protein-level cytoplasmic localization; the cited annotation evidence grade is retained and not extended to unannotated partners.	cytoplasm `GO:0005737`	UniProtKB:P77555 Source assertion: The protein is annotated in the cytoplasm (SL-0086). Evidence: ECO:0000305. Source location `comments[5] SUBCELLULAR LOCATION`
Carbamate kinase `UniProtKB:P37306`	located_in Protein-level cytoplasmic localization; the cited annotation evidence grade is retained and not extended to unannotated partners.	cytoplasm `GO:0005737`	UniProtKB:P37306 Source assertion: The protein is annotated in the cytoplasm (SL-0086). Evidence: ECO:0000305. Source location `comments[6] SUBCELLULAR LOCATION`

References

MetaCyc:PWY0-41 MetaCyc PWY0-41 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:PWY-5698 MetaCyc PWY-5698 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:CPLX-64 MetaCyc CPLX-64 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:CPLX-7524 MetaCyc CPLX-7524 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:CPLX0-7993 MetaCyc CPLX0-7993 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:ALLANTOINASE-RXN MetaCyc ALLANTOINASE-RXN (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:ALLANTOATE-DEIMINASE-RXN MetaCyc ALLANTOATE-DEIMINASE-RXN (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:URUR-RXN MetaCyc URUR-RXN (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:RXN0-7024 MetaCyc RXN0-7024 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:OXAMATE-CARBAMOYLTRANSFERASE-RXN MetaCyc OXAMATE-CARBAMOYLTRANSFERASE-RXN (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:RXN-14196 MetaCyc RXN-14196 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
MetaCyc:RXN0-5222 MetaCyc RXN0-5222 (source version: 22.5; official mirror retrieved 2026-10-10 (America/Los_Angeles))
UniProtKB:P77671 Reviewed UniProtKB P77671 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:P77425 Reviewed UniProtKB P77425 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:P75713 Reviewed UniProtKB P75713 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:P77555 Reviewed UniProtKB P77555 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:Q47208 Reviewed UniProtKB Q47208 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:P77129 Reviewed UniProtKB P77129 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:P0AAS5 Reviewed UniProtKB P0AAS5 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
UniProtKB:P37306 Reviewed UniProtKB P37306 (source version: 2026_03 (2026-09-02); retrieved 2026-10-10)
PMID:11092864 Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli. (source version: full article HTML; retrieved 2026-10-10 (America/Los_Angeles))
PMID:12486048 Metal ion dependence of recombinant Escherichia coli allantoinase. (source version: full article HTML; retrieved 2026-10-10 (America/Los_Angeles))
PMID:17362992 Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. (source version: Europe PMC core batch JSON; whole-response digest; abstract inspected; retrieved 2026-10-10 (America/Los_Angeles))
PMID:20038185 Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. (source version: Europe PMC core batch JSON; whole-response digest; abstract inspected; retrieved 2026-10-10 (America/Los_Angeles))
PMID:19935661 Ureide catabolism in Arabidopsis thaliana and Escherichia coli. (source version: Europe PMC core batch JSON; whole-response digest; abstract inspected; retrieved 2026-10-10 (America/Los_Angeles))
PMID:23284870 Structural and Functional Insights into (S)-Ureidoglycolate Dehydrogenase, a Metabolic Branch Point Enzyme in Nitrogen Utilization (source version: full article XML; supplemental Figure S2 independently inspected; retrieved 2026-10-10 (America/Los_Angeles))
PMID:38888336 Oxamic transcarbamylase of Escherichia coli is encoded by the three genes allFGH (formerly fdrA, ylbE, and ylbF) (source version: full article XML; retrieved 2026-10-10 (America/Los_Angeles))
PMID:36384810 The ybcF Gene of Escherichia coli Encodes a Local Orphan Enzyme, Catabolic Carbamate Kinase (source version: full article XML; retrieved 2026-10-10 (America/Los_Angeles))
RHEA:17029 Rhea 17029 reaction family, selected direction 17030 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)
RHEA:27485 Rhea 27485 reaction family, selected direction 27486 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)
RHEA:25241 Rhea 25241 reaction family, selected direction 25242 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)
RHEA:15329 Rhea 15329 reaction family, selected direction 15330 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)
RHEA:22984 Rhea 22984 reaction family, selected direction 22986 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)
RHEA:30755 Rhea 30755 reaction family, selected direction 30757 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)
RHEA:15649 Rhea 15649 reaction family, selected direction 15650 (source version: 142 (2026-09-02); SHA256 is the complete compressed RDF gzip)

Curation history

2026-10-11T00:10:57Z codex
- CREATE — Add the complete anaerobic allantoin-to-oxamate route with joint AllFGH evidence
  Created exact MetaCyc PWY0-41 with seven reactions, current AllC plus AllE chemistry, NAD-specific AllD, joint AllFGH gene-product roles, AllK ATP formation and separate spontaneous carbamate decomposition to the native CO2 endpoint. Retained verified AllB/AllC/AllD assemblies, alternative-metal conditions and MG1655 evidence without inventing an AllFGH complex identifier or subunit copy numbers. Native reaction cross-reference conflicts and reverse biochemical assay versus physiological direction are explicit. Author identity, 31-side and seven-balance checks passed; the independent scientific review and full final corpus gates follow before publication. Evidence: research/pathway_additions/2026-10-10-salvage/allantoin-curation.md and allantoin-validation.json.
Read this curation session