ID A0A0N4Z480_PARTI Unreviewed; 437 AA.
AC A0A0N4Z480;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase {ECO:0000256|ARBA:ARBA00013201, ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201, ECO:0000256|PIRNR:PIRNR018169};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000180100.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000180100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000256|PIRNR:PIRNR018169};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0N4Z480; -.
DR STRING; 131310.A0A0N4Z480; -.
DR WBParaSite; PTRK_0000180100.1; PTRK_0000180100.1; PTRK_0000180100.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR PANTHER; PTHR10272:SF0; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR018169};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR018169};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR018169}.
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 437 AA; 49867 MW; 8980371D0B7492A4 CRC64;
MGLIYSLPYT GEYSPKLPII GLGKYKVSCS DLMIDGGNDS IKINDEGKKE IDKKLGTFVR
LYYPNKINDF VSDGKENSDK EKKKYPLWVP RTEYFTGLAD YQEMSRIKLR TMMNMVVGQR
RIPATWQEKL IEGEDNNISD KFPVIIFSHG LSGCRHFYTV VCTALASYGY IVAALEHRDL
TSCWTYKLSY DNDCKHKIET SIPMRMVVSE YKDIKLRGKQ VMTRVKEYED LFNVLEQLNI
GALGTSQSRV LLGDEFDWGQ FTNKLDLSNT FLVGHSFGAT SAIAALGKTD LFKAAVCLDA
WMDPIKVNML HNIDKPCLFF NIESFQFPEN VKRILVVNKD GNKRNGFMYT FKDAVHQSFS
DFSFIHPGYI GKAAGLQGSV DPLHIGEVTM EMIHSYFQKL IIDEDAKESL EDIRKRYDFI
VNGTTLEVNN CELVEKL
//