ID A0A0V0UAU3_9BILA Unreviewed; 413 AA.
AC A0A0V0UAU3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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};
GN Name=PLA2G7 {ECO:0000313|EMBL:KRX48441.1};
GN ORFNames=T05_9685 {ECO:0000313|EMBL:KRX48441.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX48441.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX48441.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX48441.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX48441.1}.
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DR EMBL; JYDJ01000029; KRX48441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UAU3; -.
DR STRING; 144512.A0A0V0UAU3; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 305
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 413 AA; 47106 MW; CBFBFFD636983E86 CRC64;
MGNSVNKTLP APSGPYIVGA LDVITEHTEQ GCFFRLFYPC QIDEKSNSTT EYTPWVARSK
YIDGYVFRKI FQYTIGDAMV PAKWMQPCCS LDGTCSDAKY PLIIFSHGLG GNRLVYSAVC
TELASHGYIV AAIEHRDGSA SYTYYHELSE SSDENEIYKE KDLFFETYEP KADIFEYRNN
QLKKRVEECI KVKNYLIAKD TLEHLTELKN LKSHIDPTRI VAVGHSFGGA SVIGSLALDS
DFNAGIVLDG WMFPVDKEAE NEVQQPLLFV NNEKFQWKEN VERMQNVISK FPSGRMMYTI
KGSVHQSHAD FTHLADPWLG GFFKVRGSID PQLCHEINSK MCLHFLQKYL GLSTSESTET
DILVEFGEWR KLHNVLLFDV SASSRLRLKR THRGQQCGLT HLKWKHDPQS SHR
//
