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Database: UniProt
Entry: A0A0N4Z480_PARTI
LinkDB: A0A0N4Z480_PARTI
Original site: A0A0N4Z480_PARTI 
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};
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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
//
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