ID A0A150V954_9PEZI Unreviewed; 663 AA.
AC A0A150V954;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_63884 {ECO:0000313|EMBL:KYG47082.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47082.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG47082.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG47082.1,
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:KYG47082.1}.
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DR EMBL; JPDO01000091; KYG47082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V954; -.
DR STRING; 766039.A0A150V954; -.
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 CDD; cd00147; cPLA2_like; 1.
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:SF40; LYSOPHOSPHOLIPASE; 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}.
FT DOMAIN 52..655
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 663 AA; 74524 MW; 1ABF0521D0759A61 CRC64;
MGLREKFAGV IVPIWLRQLP LWLNKIQNEL SMAPWSLSWE IWEEAHDPEV NPEIIWDAGV
RVSTDLCPEE IVFLHNRRQY TARALARYLG VPESEIHPDD VPVIAMCGSG GGLRALVAGA
SSYLSAAEEG LWDCVTYSAG VSGSCWLQTL YYSSIGRQNY EHIIRHLKDR LGVHIAYPPA
LLGLLSTAPT NKYLLKGLIE KLKGVPDADF GLVDVYGLAL AARLLVPKME LLVSDNDLKV
SNQRFYTDSG HQPLPIYTAV RHEIPQAEDK IDEKVKNDRA STKLHDWFQW FEWTPYEMFC
EDFDAGIPTW AVGRTWQNGH CVWRQNGFAL PELRIPLMMG IWGSAFCATL SHYYKEIRPM
LQSSGFGGLD TLLAGKNDEL VKVHPIDAAV IPNFALGMRN RLPPSCPESI HESTHLQLMD
AGMANNLPIY PLLRPGRNVD IIIAFDASAD VRGDNWIRAV DGYVRQRNIK GWPMGAGWPP
DTNTAEETAN ELDQAQDAAA STNNTYQASR MSKAEAADLG FCTVWAGSTE ELQDCMDEPI
PKRIQSPDDA TQHLMSPKAG IAVVYFPFLA NPKVPGVDPL KSDFMSTWNF IYTSEQIDKV
VQLARANFEE GKEQTKRTVR AVWERKRMLR LQKEAETREH MQQQRLRTAR AAVRKHGDPF
SGL
//
