ID A0A1J8QDI4_9AGAM Unreviewed; 639 AA.
AC A0A1J8QDI4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=AZE42_08958 {ECO:0000313|EMBL:OJA18011.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA18011.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA18011.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA18011.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OJA18011.1}.
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DR EMBL; LVVM01001690; OJA18011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QDI4; -.
DR STRING; 180088.A0A1J8QDI4; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000183567; 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:UP000183567};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 23..639
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5011819888"
FT DOMAIN 36..608
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 639 AA; 67718 MW; 4BD1E07EA7BDF745 CRC64;
MLQIRFVVLL AIFPWLGIFV TAQDVSSQAY TPVAAPCPAG FNLVRMAGTP GSQSISTSEA
SYVSTRKTNV LPQAWKTYLS NVLSTNASLP AYVATILSGN SSEIPTLGIA TSGGGYRAAI
FGAGVLNALD GRNSSSTSAG IGGLLQSATY LSGLSGGSWL LTSLAQANFP TIQELAFGPT
SPTVSNNSWG GWNADYDIAT PSDNSVTDME YYTNLVEELR GKYDAGYVVT FADFWARALA
RHFTNGTFPS NFFDESYTHG AGILWSGVAN TTSFMSYSIP FPIVVADLQA PDQNSSEIIT
GDEIPLTNPI MEFNVFEMGT FDPQLSAFTP TKYLGTTNNS ICITNYDQSS LVAGSSSELF
NTYNLTNTFN SSFGPILSLM ADLLPEPKVE YDVASWPNPF YGVAPETFID SAQTNLNLVD
GGEDGEVIPL QPLLVKARGV DVIFAIDATS DINNFADGSS LIATQNRTSI YPSAYSFPLV
PTSLGEFTAQ NLTTSPTFFG CNTTSSNVST PLLIYLANGG PPHDGEAPVT NTSTSQLSYA
SSVVQEMLSQ TFVIATQGYP ADGATKDPDW PSCLACAIVD RARERAGEAR SGICSTCMNR
YCWNGSTLAT ATSGGARRIS ISHSFGLVVA SAVAAVMLM
//