ID A0A0D2B225_9EURO Unreviewed; 519 AA.
AC A0A0D2B225;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN ORFNames=PV08_09933 {ECO:0000313|EMBL:KIW12655.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW12655.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW12655.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW12655.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
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 -!- SIMILARITY: Belongs to the serine esterase family.
CC {ECO:0000256|PIRNR:PIRNR018169}.
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DR EMBL; KN847498; KIW12655.1; -; Genomic_DNA.
DR RefSeq; XP_016232871.1; XM_016384248.1.
DR AlphaFoldDB; A0A0D2B225; -.
DR STRING; 91928.A0A0D2B225; -.
DR GeneID; 27337016; -.
DR VEuPathDB; FungiDB:PV08_09933; -.
DR HOGENOM; CLU_022501_3_0_1; -.
DR OrthoDB; 2787776at2759; -.
DR Proteomes; UP000053328; 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:SF11; PHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR10272; 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|PIRNR:PIRNR018169};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR018169};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 407
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 519 AA; 57376 MW; 54059EEB30E97916 CRC64;
MGSMIWNRMV LRLPPILRPR WTWRYLLCFS VATVAIYNFL LARPLLSSNL PPYTGPYQVG
TLDLEAPCEP RRINDATLKD GQHPAFEVET VLFTLYYPSV DGASSSKPHH LWVPRPLGIV
GAGYARFARI SNFLTNSVMT FALWALAGSI KIPAHVDVPL HHGPAVLQTP AGTSSVEVDE
GFPVLVFSHG MASSRTQYTQ YCGELASRGH VVAAIEHRDG SGPGTLIMSP SGRHRTLLHF
SHRDLHHDAG LDADTFKQAQ LDFRQAEVEE TVRVLKQINA GHGDRIFSQN SRGEGQHLKH
WRGRLAMNNT TIGGHSFGAT LALQTLKGGP TIHLPFQSAV VLDPGKQSGP LNHDVNVSTL
VIHSNSWSSR YSIFYGRPHF ETVKDVVLGV LERGKAAWFM TSLGTSHPSV TDAPLIEPLL
LNWATGSSID AHEGVRQYVK VSEMFLQYQT SGVKKGILSE CVTHPEYNLP EEGRFEKGKP
SNEDMWKYWQ IHAAPCGPEA FENESEGTLY PETNPLLNG
//