| IED ID | IndEnz0005000784 |
| Enzyme Type ID | lipase000784 |
| Protein Name |
Platelet-activating factor acetylhydrolase IB subunit alpha2 EC 3.1.1.47 PAF acetylhydrolase 30 kDa subunit PAF-AH 30 kDa subunit PAF-AH subunit beta PAFAH subunit beta |
| Gene Name | PAFAH1B2 PAFAHB |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA |
| Enzyme Length | 229 |
| Uniprot Accession Number | P68402 |
| Absorption | |
| Active Site | ACT_SITE 48; /evidence=ECO:0000250; ACT_SITE 193; /evidence=ECO:0000250; ACT_SITE 196; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Beta subunit (PAFAH1B1) stimulates the acetylhydrolase activity of the alpha2/alpha2 catalytic homodimer. {ECO:0000250|UniProtKB:P68401}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000250|UniProtKB:P68401};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000250|UniProtKB:P68401}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P68401};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000250|UniProtKB:P68401}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-hexadecyl-sn-glycero-3-phosphate + acetate + H(+); Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385; Evidence={ECO:0000250|UniProtKB:P68401};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; Evidence={ECO:0000250|UniProtKB:P68401}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphoethanolamine + acetate + H(+); Xref=Rhea:RHEA:41708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:78387, ChEBI:CHEBI:78390; Evidence={ECO:0000250|UniProtKB:P68401};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709; Evidence={ECO:0000250|UniProtKB:P68401}; |
| DNA Binding | |
| EC Number | 3.1.1.47 |
| Enzyme Function | FUNCTION: Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (By similarity). May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity). {ECO:0000250|UniProtKB:P68401, ECO:0000250|UniProtKB:Q61206}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (3); Beta strand (9); Chain (1); Helix (9); Initiator methionine (1); Modified residue (4); Sequence conflict (2); Turn (2) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Phosphoprotein;Reference proteome |
| Interact With | Q5SYC1; Q15102; O60260-5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"; MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 220; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q61206" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1VYH; |
| Mapped Pubmed ID | 10359595; 11080672; 12432908; 16169070; 16189514; 17353931; 17849047; 18464913; 18641641; 19019335; 19622634; 19738201; 19753100; 20360068; 20420828; 21844189; 21866060; 22130221; 23238734; 23508960; 23650620; 25034894; 25814554; 25945974; 26496610; 27910906; 29758199; 9671731; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,569 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17777; RHEA:17778; RHEA:40479; RHEA:40480; RHEA:41704; RHEA:41705; RHEA:41708; RHEA:41709 |
| Cross Reference Brenda | 3.1.1.47; |