ID A0A0D2A3Z5_9PEZI Unreviewed; 535 AA.
AC A0A0D2A3Z5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=PV09_07239 {ECO:0000313|EMBL:KIW01190.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW01190.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW01190.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW01190.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847556; KIW01190.1; -; Genomic_DNA.
DR RefSeq; XP_016211059.1; XM_016360983.1.
DR AlphaFoldDB; A0A0D2A3Z5; -.
DR STRING; 253628.A0A0D2A3Z5; -.
DR GeneID; 27315212; -.
DR VEuPathDB; FungiDB:PV09_07239; -.
DR HOGENOM; CLU_013227_1_0_1; -.
DR InParanoid; A0A0D2A3Z5; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000053259; 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:SF40; LYSOPHOSPHOLIPASE; 1.
DR Pfam; PF01735; PLA2_B; 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:UP000053259}.
FT DOMAIN 1..535
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 535 AA; 59881 MW; 98BBC1B7F9AB7CD3 CRC64;
MAIDPQEVHP DDVPTIALGG SGGGLRAMIT VLGFCNESKK AKLWDTFTYV AGTSGSCWSL
AAYYTFGEAS MSKVIEHCKH RLHPHHPFSY HAIRELLTKG AYATLGPLIQ KRKSGLNTVA
MDFYSVLTTG YLFLHKDPAL TPGGPGLDTK KEVAGYHSEW FKWSNALLQD GKQPLPILTA
VRHERPWITS GVMQDSWFQW FEMTPFEVGC DELQAWVPTW GFGRPFYGGK SQTQLPEQSL
ALLLGLCTSA PAAHLKSYVD VIERNLSSGF FGNLIRAIAR RVTTFWGEQG MRIFQMHHPI
HACNEHNFLF RLNANDKSKS ETDADLSIAQ FPRLHLIDAG VDNNCPTYVL LHPSRKVDVI
ITVDASSDVR RNLFQTNINR IGSRRKLQFC KRSSPKKDGS TNESGCLKDM YAQIYDGTIM
EHRPETVVDL YGNVIVNPPA PPSKKDCTMI YVPLLPNENA VKGFDPLTAK FARSFNLIWT
PEQVESLTQV AAANFREGEE TIKAVLLETW LKKKAMRESR GDSLSTTQKI NEAVR
//
