Detail Information for IndEnz0010001381
IED ID IndEnz0010001381
Enzyme Type ID esterase001381
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;