ID A0A150V5X8_9PEZI Unreviewed; 578 AA.
AC A0A150V5X8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN ORFNames=M433DRAFT_134283 {ECO:0000313|EMBL:KYG45932.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG45932.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG45932.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG45932.1,
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-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|RuleBase:RU362103};
CC -!- SIMILARITY: Belongs to the lysophospholipase family.
CC {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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:KYG45932.1}.
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DR EMBL; JPDO01000138; KYG45932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V5X8; -.
DR STRING; 766039.A0A150V5X8; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU00555};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 21..578
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5007358634"
FT DOMAIN 42..576
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 578 AA; 62494 MW; DB30E11F0309B901 CRC64;
MATTVIQSFS LAALCGLAAA APAPLVNKAI RALDAYAPVT TSCPSESLVR PATSINTDEA
AYVSARKINA DSALASWLAK QGSFDTSSQP MVGFTSSGGG YRSLLETAGV VQGLDARDSN
INTSGLYQAL TYEAGLSGGS WFLSSLAGNN WPTVTYLKDN LWLDAFQNSA LLPANIFSIS
DDLMYAEIDA DLQAKSDAGY NITIVDPYGR LLSHQLLEGF DGGVSTRLSG LTAFSNFTAH
AVPFPIITTT STDLGMEGQC FPELNSPIFE FSPYEYGSWD EGVSAFAVTE YMGTAMSNGA
PSTAGQCTVY YDNLGYIFGT SSDVWNAVCE IIEPSSSSSA DLEEALEYFV SNIHAPVFQD
LFGVYPNPFY NYTRSNLVSE NSLLTLADGG ETNQNNPIWP FIQPERSVDV LIVNDNSADT
STNYPNGSEI YQTYVRAQAT GLTKMPYIPD VATFISEGLN QHATFFGCNE TDTIFIVWLP
NVDYTYDSGQ STSKVEYTKS ETEAMYVNSF GYFSLKHMLT DETHFRIANG VQIANQNGEE
GWSFCLACAI KNGDGNSLPD GCNECFSKYC YYKSGTSD
//
