ID A0A150VBN0_9PEZI Unreviewed; 515 AA.
AC A0A150VBN0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN ORFNames=M433DRAFT_84785 {ECO:0000313|EMBL:KYG47917.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47917.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG47917.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG47917.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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}.
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:KYG47917.1}.
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DR EMBL; JPDO01000062; KYG47917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VBN0; -.
DR STRING; 766039.A0A150VBN0; -.
DR Proteomes; UP000075602; 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:SF7; 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:UP000075602}.
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 400
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 515 AA; 57872 MW; 31D764D91DB971FC CRC64;
MASWLSVLNP IRHFPPYNGP YSVGTVDVEI PVSDLPSPAD APEDAQPTIA FRIFYPCIKP
EKNEYDRPVR WIPQPQRETI ASFAKFLGLG QKMAGAVSYV AQQLYWVKLP AHRNAKLLDP
PTSNRRWPVT FFSHGLAGSR NAYSQICGDL ASNGMIVISL DHRDGSSPIQ YVRATATTEA
HVVYPVKIPH HPVTDDVYEG RDKQLRIRLW EICMAFEALV KIDRGHHIEN LDSNTSRIRQ
ERMEVLWQFN DMMDIHRPGK VTWAGHSFGA ATTVQLLKSI FYYQERCEMD GKPLIIPNRD
AAIVGQIVAE SPTVLLDMWC MPLQSPSQKF LWDRPLPSFA IGGPNGANVL SILSEAFKNW
EDNLNIIKAV AAKPSLSRRP SRTKEHKSGP HMFYVARSQH FNQSDFGIVF SYIAYRVTKA
EEPEWCLALN TRAMVQVIRE SGIEVSGEDD KEILDREGGI RKWIPITVDD DEQLLSPGTD
ALVTATSARL VTCTSAPKDG MTMGEKMQSQ SEVLV
//