phosphatidylethanolamine biosynthesis I

gomodel:YeastPathways_PWY-5669

Phosphatidylethanolamine biosynthesis I in Saccharomyces cerevisiae S288C transfers phosphatidyl groups from CDP-diacylglycerol to L-serine to form 3-sn-phosphatidyl-L-serine, then decarboxylates 3-sn-phosphatidyl-L-serine through PSD1 or PSD2 to form phosphatidylethanolamine.

Pathway type
lipid biosynthesis
Organism scope

Read the source YAML

Pathway network

26 nodes · 34 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: phosphatidylethanolamine biosynthesis I 26 nodes · 34 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — has_output → CHEBI:16526; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:PHOSPHASERSYN-RXN — part_of → GO:0006646; Evidence: gomodel:YeastPathways_PWY-5669part of gomodel:PHOSPHASERSYN-RXN — has_input → CHEBI:33384; Evidence: gomodel:YeastPathways_PWY-5669has input gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — has_output → CHEBI:16038; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — has_input → CHEBI:15378; Evidence: gomodel:YeastPathways_PWY-5669has input gomodel:PHOSPHASERSYN-RXN — has_output → CHEBI:11750; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:PHOSPHASERDECARB-RXN — part_of → GO:0006646; Evidence: gomodel:YeastPathways_PWY-5669part of gomodel:PHOSPHASERDECARB-RXN — has_input → CHEBI:15378; Evidence: gomodel:YeastPathways_PWY-5669has input gomodel:PHOSPHASERDECARB-RXN — has_output → CHEBI:16526; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:PHOSPHASERSYN-RXN — has_input → CHEBI:17962; Evidence: gomodel:YeastPathways_PWY-5669has input SGD:S000003402 — enables → gomodel:YeastPathways_PWY-5669/6a46ef0600000808; Evidence: gomodel:YeastPathways_PWY-5669enables gomodel:PHOSPHASERDECARB-RXN — has_output → CHEBI:16038; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:PHOSPHASERSYN-RXN — has_output → CHEBI:60377; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — part_of → GO:0006646; Evidence: gomodel:YeastPathways_PWY-5669part of SGD:S000000828 — enables → gomodel:PHOSPHASERSYN-RXN; Evidence: gomodel:YeastPathways_PWY-5669enables gomodel:PHOSPHASERDECARB-RXN — has_input → CHEBI:11750; Evidence: gomodel:YeastPathways_PWY-5669has input SGD:S000005113 — enables → gomodel:PHOSPHASERDECARB-RXN; Evidence: gomodel:YeastPathways_PWY-5669enables gomodel:PHOSPHASERSYN-RXN — has_output → CHEBI:15378; Evidence: gomodel:YeastPathways_PWY-5669has output gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — has_input → CHEBI:11750; Evidence: gomodel:YeastPathways_PWY-5669has input SGD:S000003402 — located_in → GO:0000139; Physical protein location from reviewed UniProt. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:7890739) Topology: Peripheral membrane protein. Orientation: Cytoplasmic side.; Evidence: UniProtKB:P53037, UniProtKB:P53037located in SGD:S000003402 — located_in → GO:0010008; Physical protein location from reviewed UniProt. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:20016005) Topology: Peripheral membrane protein. Orientation: Cytoplasmic side.; Evidence: UniProtKB:P53037, UniProtKB:P53037located in SGD:S000000828 — located_in → GO:0005789; Physical protein location from reviewed UniProt. evidence code not specified by source Topology: Multi-pass membrane protein.; Evidence: UniProtKB:P08456, UniProtKB:P08456located in SGD:S000000828 — located_in → GO:0005741; Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:3005242) Topology: Multi-pass membrane protein.; Evidence: UniProtKB:P08456, UniProtKB:P08456located in SGD:S000005113 — located_in → GO:0005743; Physical protein location from reviewed UniProt. ECO:0000255 (HAMAP-Rule:MF_03208); ECO:0000269 (PubMed:14576278); ECO:0000269 (PubMed:22984266); ECO:0000269 (PubMed:23124206); ECO:0000269 (PubMed:29290583); ECO:0000269 (PubMed:3005242); ECO:0000269 (PubMed:33718843); ECO:0000305 (PubMed:34818062); molecular form: Phosphatidylserine decarboxylase 1 beta chain. Topology: Single-pass membrane protein. Orientation: Intermembrane side.; Evidence: UniProtKB:P39006, UniProtKB:P39006, UniProtKB:P39006located in SGD:S000005113 — located_in → GO:0005811; Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:34818062) Source qualification: Localizes to sites of lipid droplet formation on the endoplasmic reticulum membrane; Evidence: UniProtKB:P39006, UniProtKB:P39006located in SGD:S000005113 — located_in → GO:0005789; Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:29290583); ECO:0000269 (PubMed:34818062) Source qualification: Localizes to sites of lipid droplet formation on the endoplasmic reticulum membrane; Evidence: UniProtKB:P39006, UniProtKB:P39006located in gomodel:PHOSPHASERDECARB-RXN — occurs_in → GO:0005739; Activity compartment supported by an inspected functional annotation. ECO:0000255 (HAMAP-Rule:MF_03208); ECO:0000269 (PubMed:11294902); ECO:0000269 (PubMed:17976194); ECO:0000269 (PubMed:23045528); ECO:0000269 (PubMed:23124206); ECO:0000269 (PubMed:25829489); ECO:0000269 (PubMed:29290583); ECO:0000269 (PubMed:30926815); ECO:0000269 (PubMed:34818062); ECO:0000269 (PubMed:8227017); ECO:0000269 (PubMed:8407984); ECO:0000269 (PubMed:8530379). Alternative isoenzymes may function elsewhere.; Evidence: UniProtKB:P39006occurs in gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — occurs_in → GO:0000139; Activity compartment supported by an inspected functional annotation. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:11294902); ECO:0000269 (PubMed:20016005); ECO:0000269 (PubMed:24366873); ECO:0000269 (PubMed:7890739); ECO:0000269 (PubMed:7890740). Alternative isoenzymes may function elsewhere.; Evidence: UniProtKB:P53037occurs in gomodel:YeastPathways_PWY-5669/6a46ef0600000808 — occurs_in → GO:0010008; Activity compartment supported by an inspected functional annotation. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:11294902); ECO:0000269 (PubMed:20016005); ECO:0000269 (PubMed:24366873); ECO:0000269 (PubMed:7890739); ECO:0000269 (PubMed:7890740). Alternative isoenzymes may function elsewhere.; Evidence: UniProtKB:P53037occurs in SGD:S000003402 — has_cofactor → CHEBI:45360; UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The cofactor note explicitly describes a covalently bound pyruvoyl group; use the exact group class rather than free pyruvate. UniProt evidence: ECO:0000250 (UniProtKB:P0A8K1); ECO:0000255 (HAMAP-Rule:MF_03209) Binds 1 pyruvoyl group covalently per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P0A8K1); ECO:0000255 (HAMAP-Rule:MF_03209); Evidence: CHEBI:45360, UniProtKB:P53037, UniProtKB:P53037has cofactor SGD:S000003402 — has_cofactor → CHEBI:29108; UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The cofactor note explicitly describes a covalently bound pyruvoyl group; use the exact group class rather than free pyruvate. UniProt evidence: ECO:0000255 (PROSITE-ProRule:PRU00041); Evidence: UniProtKB:P53037, UniProtKB:P53037has cofactor SGD:S000000828 — has_cofactor → CHEBI:29035; UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:6088519); ECO:0000269 (PubMed:6274497) Divalent metal cations; Mn(2+) or Mg(2+). UniProt note evidence: ECO:0000269 (PubMed:6088519); Evidence: UniProtKB:P08456, UniProtKB:P08456has cofactor SGD:S000000828 — has_cofactor → CHEBI:18420; UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:6088519) Divalent metal cations; Mn(2+) or Mg(2+). UniProt note evidence: ECO:0000269 (PubMed:6088519); Evidence: UniProtKB:P08456, UniProtKB:P08456has cofactor SGD:S000005113 — has_cofactor → CHEBI:45360; UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The cofactor note explicitly describes a covalently bound pyruvoyl group; use the exact group class rather than free pyruvate. UniProt evidence: ECO:0000255 (HAMAP-Rule:MF_03208) Binds 1 pyruvoyl group covalently per subunit. UniProt note evidence: ECO:0000255 (HAMAP-Rule:MF_03208); Evidence: CHEBI:45360, UniProtKB:P39006, UniProtKB:P39006has cofactor carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide phosphatidylethanolamine biosynthetic process; GO:0006646; Declared type: biological_process biological process phosphatidylethanolamine biosynthetic process L-serine zwitterion; CHEBI:33384; Declared type: small_molecule small molecule L-serine zwitterion phosphatidylethanolamine; CHEBI:16038; Declared type: lipid lipid phosphatidylethanolamine cytosol; GO:0005829; Declared type: cellular_component cellular component cytosol hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron 3-sn-phosphatidyl-L-serine; CHEBI:11750; Declared type: lipid lipid 3-sn-phosphatidyl-L-serine CDP-diacylglycerol; CHEBI:17962; Declared type: lipid lipid CDP-diacylglycerol PSD2 Scer; SGD:S000003402; Declared type: protein protein PSD2 Scer cytidine 5'-monophosphate(2-); CHEBI:60377; Declared type: small_molecule small molecule cytidine 5'-monophosphate(2-) CHO1 Scer; SGD:S000000828; Declared type: protein protein CHO1 Scer PSD1 Scer; SGD:S000005113; Declared type: protein protein PSD1 Scer Golgi membrane; GO:0000139; Declared type: cellular_component cellular component Golgi membrane endosome membrane; GO:0010008; Declared type: cellular_component cellular component endosome membrane endoplasmic reticulum membrane; GO:0005789; Declared type: cellular_component cellular component endoplasmic reticulum membrane mitochondrial outer membrane; GO:0005741; Declared type: cellular_component cellular component mitochondrial outer membrane mitochondrial inner membrane; GO:0005743; Declared type: cellular_component cellular component mitochondrial inner membrane lipid droplet; GO:0005811; Declared type: cellular_component cellular component lipid droplet mitochondrion; GO:0005739; Declared type: cellular_component cellular component mitochondrion pyruvoyl group; CHEBI:45360; Declared type: cofactor cofactor pyruvoyl group calcium(2+); CHEBI:29108; Declared type: cofactor cofactor calcium(2+) manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) phosphatidylserine decarboxylase activity; gomodel:PHOSPHASERDECARB-RXN; Declared type: molecular_activity molecular activity phosphatidylserine decarboxylase activity CDP-diacylglycerol-serine O-phosphatidyltransferase activity; gomodel:PHOSPHASERSYN-RXN; Declared type: molecular_activity molecular activity CDP-diacylglycerol-serine O-phosphatidyltransferase activity phosphatidylserine decarboxylase activity (PSD2); gomodel:YeastPathways_PWY-5669/6a46ef0600000808; Declared type: molecular_activity molecular activity phosphatidylserine decarboxylase activity (PSD2)

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Saccharomyces cerevisiae S288C
NCBITaxon:559292		taxon
carbon dioxide
CHEBI:16526		small molecule
phosphatidylethanolamine biosynthetic process
GO:0006646		biological process
L-serine zwitterion
CHEBI:33384		small molecule
phosphatidylethanolamine
CHEBI:16038		lipid
cytosol
GO:0005829		cellular component
hydron
CHEBI:15378		small molecule
3-sn-phosphatidyl-L-serine
CHEBI:11750		lipid
CDP-diacylglycerol
CHEBI:17962		lipid
PSD2 Scer
SGD:S000003402		protein
cytidine 5'-monophosphate(2-)
CHEBI:60377		small molecule
CHO1 Scer
SGD:S000000828		protein
PSD1 Scer
SGD:S000005113		protein
Golgi membrane
GO:0000139		cellular component
endosome membrane
GO:0010008		cellular component
endoplasmic reticulum membrane
GO:0005789		cellular component
mitochondrial outer membrane
GO:0005741		cellular component
mitochondrial inner membrane
GO:0005743		cellular component
lipid droplet
GO:0005811		cellular component
mitochondrion
GO:0005739		cellular component
pyruvoyl group
CHEBI:45360		cofactor
calcium(2+)
CHEBI:29108		cofactor
manganese(2+)
CHEBI:29035		cofactor
magnesium(2+)
CHEBI:18420		cofactor
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		molecular activity
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		molecular activity
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		molecular activity

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		has_output

carbon dioxide
CHEBI:16526
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:YeastPathways_PWY-5669/6a46ef0600000808 RO:0002234 gomodel:YeastPathways_PWY-5669/6a46ef0600000810.

    Source location./YeastPathways_PWY-5669.json#/facts/0; endpoint types: /individuals/28/type; /individuals/30/type
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		part_of

phosphatidylethanolamine biosynthetic process
GO:0006646
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN BFO:0000050 gomodel:YeastPathways_PWY-5669/YeastPathways_PWY-5669.

    Source location./YeastPathways_PWY-5669.json#/facts/1; endpoint types: /individuals/9/type; /individuals/27/type
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		has_input

L-serine zwitterion
CHEBI:33384
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN RO:0002233 gomodel:CHEBI_33384_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/2; endpoint types: /individuals/9/type; /individuals/6/type
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		has_output

phosphatidylethanolamine
CHEBI:16038
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:YeastPathways_PWY-5669/6a46ef0600000808 RO:0002234 gomodel:YeastPathways_PWY-5669/6a46ef0600000811.

    Source location./YeastPathways_PWY-5669.json#/facts/3; endpoint types: /individuals/28/type; /individuals/31/type
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		has_input

hydron
CHEBI:15378
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:YeastPathways_PWY-5669/6a46ef0600000808 RO:0002233 gomodel:YeastPathways_PWY-5669/6a46ef0600000809.

    Source location./YeastPathways_PWY-5669.json#/facts/5; endpoint types: /individuals/28/type; /individuals/29/type
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		has_output

3-sn-phosphatidyl-L-serine
CHEBI:11750
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN RO:0002234 gomodel:CHEBI_11750_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/6; endpoint types: /individuals/9/type; /individuals/0/type
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		part_of

phosphatidylethanolamine biosynthetic process
GO:0006646
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERDECARB-RXN BFO:0000050 gomodel:YeastPathways_PWY-5669/YeastPathways_PWY-5669.

    Source location./YeastPathways_PWY-5669.json#/facts/7; endpoint types: /individuals/8/type; /individuals/27/type
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		has_input

hydron
CHEBI:15378
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERDECARB-RXN RO:0002233 gomodel:CHEBI_15378_PHOSPHASERDECARB-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/8; endpoint types: /individuals/8/type; /individuals/1/type
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		has_output

carbon dioxide
CHEBI:16526
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERDECARB-RXN RO:0002234 gomodel:CHEBI_16526_PHOSPHASERDECARB-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/9; endpoint types: /individuals/8/type; /individuals/4/type
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		has_input

CDP-diacylglycerol
CHEBI:17962
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN RO:0002233 gomodel:CHEBI_17962_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/11; endpoint types: /individuals/9/type; /individuals/5/type
PSD2 Scer
SGD:S000003402		enables

phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:YeastPathways_PWY-5669/6a46ef0600000808 RO:0002333 gomodel:YeastPathways_PWY-5669/6a46ef0600000812.

    Source location./YeastPathways_PWY-5669.json#/facts/12; endpoint types: /individuals/28/type; /individuals/32/type
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		has_output

phosphatidylethanolamine
CHEBI:16038
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERDECARB-RXN RO:0002234 gomodel:CHEBI_16038_PHOSPHASERDECARB-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/13; endpoint types: /individuals/8/type; /individuals/3/type
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		has_output

cytidine 5'-monophosphate(2-)
CHEBI:60377
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN RO:0002234 gomodel:CHEBI_60377_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/15; endpoint types: /individuals/9/type; /individuals/7/type
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		part_of

phosphatidylethanolamine biosynthetic process
GO:0006646
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:YeastPathways_PWY-5669/6a46ef0600000808 BFO:0000050 gomodel:YeastPathways_PWY-5669/YeastPathways_PWY-5669.

    Source location./YeastPathways_PWY-5669.json#/facts/16; endpoint types: /individuals/28/type; /individuals/27/type
CHO1 Scer
SGD:S000000828		enables

CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN RO:0002333 gomodel:YER026C-MONOMER_PHOSPHASERSYN-RXN_controller.

    Source location./YeastPathways_PWY-5669.json#/facts/17; endpoint types: /individuals/9/type; /individuals/10/type
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		has_input

3-sn-phosphatidyl-L-serine
CHEBI:11750
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERDECARB-RXN RO:0002233 gomodel:CHEBI_11750_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/18; endpoint types: /individuals/8/type; /individuals/0/type
PSD1 Scer
SGD:S000005113		enables

phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERDECARB-RXN RO:0002333 gomodel:YNL169C-MONOMER_PHOSPHASERDECARB-RXN_controller.

    Source location./YeastPathways_PWY-5669.json#/facts/19; endpoint types: /individuals/8/type; /individuals/11/type
CDP-diacylglycerol-serine O-phosphatidyltransferase activity
gomodel:PHOSPHASERSYN-RXN		has_output

hydron
CHEBI:15378
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:PHOSPHASERSYN-RXN RO:0002234 gomodel:CHEBI_15378_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/20; endpoint types: /individuals/9/type; /individuals/2/type
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		has_input

3-sn-phosphatidyl-L-serine
CHEBI:11750
  • gomodel:YeastPathways_PWY-5669

    Source assertion: The model asserts gomodel:YeastPathways_PWY-5669/6a46ef0600000808 RO:0002233 gomodel:CHEBI_11750_PHOSPHASERSYN-RXN.

    Source location./YeastPathways_PWY-5669.json#/facts/21; endpoint types: /individuals/28/type; /individuals/0/type
PSD2 Scer
SGD:S000003402		located_in

Physical protein location from reviewed UniProt. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:7890739) Topology: Peripheral membrane protein. Orientation: Cytoplasmic side.

Golgi membrane
GO:0000139
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 annotates location Golgi apparatus membrane (SL-0134).

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/2090/comments/1/subcellularLocations/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 has the exact SGD cross-reference SGD:S000003402.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/2090/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
PSD2 Scer
SGD:S000003402		located_in

Physical protein location from reviewed UniProt. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:20016005) Topology: Peripheral membrane protein. Orientation: Cytoplasmic side.

endosome membrane
GO:0010008
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 annotates location Endosome membrane (SL-0100).

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/2090/comments/1/subcellularLocations/1; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 has the exact SGD cross-reference SGD:S000003402.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/2090/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
CHO1 Scer
SGD:S000000828		located_in

Physical protein location from reviewed UniProt. evidence code not specified by source Topology: Multi-pass membrane protein.

endoplasmic reticulum membrane
GO:0005789
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 annotates location Endoplasmic reticulum membrane (SL-0097).

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/205/comments/1/subcellularLocations/1; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 has the exact SGD cross-reference SGD:S000000828.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/205/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
CHO1 Scer
SGD:S000000828		located_in

Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:3005242) Topology: Multi-pass membrane protein.

mitochondrial outer membrane
GO:0005741
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 annotates location Mitochondrion outer membrane (SL-0172).

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/205/comments/1/subcellularLocations/2; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 has the exact SGD cross-reference SGD:S000000828.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/205/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
PSD1 Scer
SGD:S000005113		located_in

Physical protein location from reviewed UniProt. ECO:0000255 (HAMAP-Rule:MF_03208); ECO:0000269 (PubMed:14576278); ECO:0000269 (PubMed:22984266); ECO:0000269 (PubMed:23124206); ECO:0000269 (PubMed:29290583); ECO:0000269 (PubMed:3005242); ECO:0000269 (PubMed:33718843); ECO:0000305 (PubMed:34818062); molecular form: Phosphatidylserine decarboxylase 1 beta chain. Topology: Single-pass membrane protein. Orientation: Intermembrane side.

mitochondrial inner membrane
GO:0005743
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 annotates location Mitochondrion inner membrane (SL-0168); molecular form: Phosphatidylserine decarboxylase 1 beta chain.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/comments/1/subcellularLocations/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 has the exact SGD cross-reference SGD:S000005113.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 annotates location Mitochondrion inner membrane (SL-0168); molecular form: Phosphatidylserine decarboxylase 1 alpha chain.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/comments/2/subcellularLocations/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
PSD1 Scer
SGD:S000005113		located_in

Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:34818062) Source qualification: Localizes to sites of lipid droplet formation on the endoplasmic reticulum membrane

lipid droplet
GO:0005811
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 annotates location Lipid droplet (SL-0154).

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/comments/3/subcellularLocations/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 has the exact SGD cross-reference SGD:S000005113.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
PSD1 Scer
SGD:S000005113		located_in

Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:29290583); ECO:0000269 (PubMed:34818062) Source qualification: Localizes to sites of lipid droplet formation on the endoplasmic reticulum membrane

endoplasmic reticulum membrane
GO:0005789
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 annotates location Endoplasmic reticulum membrane (SL-0097).

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/comments/3/subcellularLocations/1; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 has the exact SGD cross-reference SGD:S000005113.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/uniProtKBCrossReferences/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
phosphatidylserine decarboxylase activity
gomodel:PHOSPHASERDECARB-RXN		occurs_in

Activity compartment supported by an inspected functional annotation. ECO:0000255 (HAMAP-Rule:MF_03208); ECO:0000269 (PubMed:11294902); ECO:0000269 (PubMed:17976194); ECO:0000269 (PubMed:23045528); ECO:0000269 (PubMed:23124206); ECO:0000269 (PubMed:25829489); ECO:0000269 (PubMed:29290583); ECO:0000269 (PubMed:30926815); ECO:0000269 (PubMed:34818062); ECO:0000269 (PubMed:8227017); ECO:0000269 (PubMed:8407984); ECO:0000269 (PubMed:8530379). Alternative isoenzymes may function elsewhere.

mitochondrion
GO:0005739
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 describes the corresponding catalytic function in the mitochondrion; this projection applies to the activity enabled by SGD:S000005113.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/1539/comments/0/texts/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		occurs_in

Activity compartment supported by an inspected functional annotation. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:11294902); ECO:0000269 (PubMed:20016005); ECO:0000269 (PubMed:24366873); ECO:0000269 (PubMed:7890739); ECO:0000269 (PubMed:7890740). Alternative isoenzymes may function elsewhere.

Golgi membrane
GO:0000139
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 describes the corresponding catalytic function in the Golgi membrane; this projection applies to the activity enabled by SGD:S000003402.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/2090/comments/0/texts/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
phosphatidylserine decarboxylase activity (PSD2)
gomodel:YeastPathways_PWY-5669/6a46ef0600000808		occurs_in

Activity compartment supported by an inspected functional annotation. ECO:0000255 (HAMAP-Rule:MF_03209); ECO:0000269 (PubMed:11294902); ECO:0000269 (PubMed:20016005); ECO:0000269 (PubMed:24366873); ECO:0000269 (PubMed:7890739); ECO:0000269 (PubMed:7890740). Alternative isoenzymes may function elsewhere.

endosome membrane
GO:0010008
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 describes the corresponding catalytic function in the endosome membrane; this projection applies to the activity enabled by SGD:S000003402.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_subcellular_location%2Ccc_function%2Ccc_caution%2Corganism_id#/results/2090/comments/0/texts/0; sha256=95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d
PSD2 Scer
SGD:S000003402		has_cofactor

UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The cofactor note explicitly describes a covalently bound pyruvoyl group; use the exact group class rather than free pyruvate. UniProt evidence: ECO:0000250 (UniProtKB:P0A8K1); ECO:0000255 (HAMAP-Rule:MF_03209) Binds 1 pyruvoyl group covalently per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P0A8K1); ECO:0000255 (HAMAP-Rule:MF_03209)

pyruvoyl group
CHEBI:45360
  • CHEBI:45360

    Source assertion: ChEBI labels CHEBI:45360 as pyruvoyl group.

    Source locationchebi.obo [Term] id: CHEBI:45360; name: pyruvoyl group
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 cross-references CHEBI:15361, but its note specifies a covalently bound pyruvoyl group; that group is projected to CHEBI:45360.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/2090/comments/0/cofactors/0; /results/2090/comments/0/note
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 has the exact SGD cross-reference SGD:S000003402.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/2090/uniProtKBCrossReferences/0
PSD2 Scer
SGD:S000003402		has_cofactor

UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The cofactor note explicitly describes a covalently bound pyruvoyl group; use the exact group class rather than free pyruvate. UniProt evidence: ECO:0000255 (PROSITE-ProRule:PRU00041)

calcium(2+)
CHEBI:29108
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 annotates CHEBI:29108 as a cofactor of this protein.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/2090/comments/1/cofactors/0
  • UniProtKB:P53037

    Source assertion: UniProtKB:P53037 has the exact SGD cross-reference SGD:S000003402.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/2090/uniProtKBCrossReferences/0
CHO1 Scer
SGD:S000000828		has_cofactor

UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:6088519); ECO:0000269 (PubMed:6274497) Divalent metal cations; Mn(2+) or Mg(2+). UniProt note evidence: ECO:0000269 (PubMed:6088519)

manganese(2+)
CHEBI:29035
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 annotates CHEBI:29035 as a cofactor of this protein.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/205/comments/0/cofactors/0; /results/205/comments/0/note
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 has the exact SGD cross-reference SGD:S000000828.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/205/uniProtKBCrossReferences/0
CHO1 Scer
SGD:S000000828		has_cofactor

UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:6088519) Divalent metal cations; Mn(2+) or Mg(2+). UniProt note evidence: ECO:0000269 (PubMed:6088519)

magnesium(2+)
CHEBI:18420
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 annotates CHEBI:18420 as a cofactor of this protein.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/205/comments/0/cofactors/1; /results/205/comments/0/note
  • UniProtKB:P08456

    Source assertion: UniProtKB:P08456 has the exact SGD cross-reference SGD:S000000828.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/205/uniProtKBCrossReferences/0
PSD1 Scer
SGD:S000005113		has_cofactor

UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The cofactor note explicitly describes a covalently bound pyruvoyl group; use the exact group class rather than free pyruvate. UniProt evidence: ECO:0000255 (HAMAP-Rule:MF_03208) Binds 1 pyruvoyl group covalently per subunit. UniProt note evidence: ECO:0000255 (HAMAP-Rule:MF_03208)

pyruvoyl group
CHEBI:45360
  • CHEBI:45360

    Source assertion: ChEBI labels CHEBI:45360 as pyruvoyl group.

    Source locationchebi.obo [Term] id: CHEBI:45360; name: pyruvoyl group
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 cross-references CHEBI:15361, but its note specifies a covalently bound pyruvoyl group; that group is projected to CHEBI:45360.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/1539/comments/0/cofactors/0; /results/1539/comments/0/note
  • UniProtKB:P39006

    Source assertion: UniProtKB:P39006 has the exact SGD cross-reference SGD:S000005113.

    Source locationhttps://rest.uniprot.org/uniprotkb/stream?query=taxonomy_id%3A559292+AND+reviewed%3Atrue&format=json&fields=accession%2Cprotein_name%2Cxref_sgd%2Ccc_cofactor%2Corganism_id%2Ccc_caution [sha256:1378282d22c5518215707964664b55946f468ba74a227a6ea1bbf27db69ddbc4] #/results/1539/uniProtKBCrossReferences/0

References

Curation history