ID   F4PEG7_BATDJ            Unreviewed;       466 AA.
AC   F4PEG7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE            EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN   ORFNames=BATDEDRAFT_92708 {ECO:0000313|EMBL:EGF76423.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF76423.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF76423.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) 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   -!- SIMILARITY: Belongs to the serine esterase family.
CC       {ECO:0000256|PIRNR:PIRNR018169}.
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DR   EMBL; GL882897; EGF76423.1; -; Genomic_DNA.
DR   RefSeq; XP_006683024.1; XM_006682961.1.
DR   AlphaFoldDB; F4PEG7; -.
DR   STRING; 684364.F4PEG7; -.
DR   GeneID; 18244729; -.
DR   HOGENOM; CLU_024458_0_0_1; -.
DR   InParanoid; F4PEG7; -.
DR   OMA; MGVNQSM; -.
DR   OrthoDB; 2787776at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IBA:GO_Central.
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   3: Inferred from homology;
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:UP000007241}.
SQ   SEQUENCE   466 AA;  51858 MW;  1F52C15EC0D2C544 CRC64;
     MTTNAKTPST AKTLIKPAGF SFTAKLPLYN GPFNVGMMDI ETKPLAQSDS SEIKGMPYKR
     GLLVRIYYPT TVTSNSCKKP HWLPISPLYA LGYSSFLNLP WIVGRMLVSP LTSKVTIPSY
     WQTPLAHPSD TQTTIPSIPH RLPVVVFSHG LAGMRTTYST LCGSLAAKGF IVLVPEHSDG
     SACATIRQSN SSTSTQHEHI AYLRPDKTSV LPGETTDDYL LRLRRAQVEI RADEVDACIE
     ILKKLDMGSF DPKDNLIGNH AESGPCIDSF KSRVDFQHMV MAGHSFGGAT TITVLSRPNM
     PFRCGIILDP WMFPVHNPNV TVPYLSIQSE TFHWKTNLDQ MRSMMGLVPY SNTTDSTAAS
     TVLTTSTLQH PHTRFGYIRH TAHNNPSDFS GLFPTVIQWA GQAGSADALR VYRINDDWMC
     EFIATIYEQM ELKLPRSAEY KIGQEQDEMI AVGDQAWNDL YSRLKK
//