ID A0A367XXD8_9ASCO Unreviewed; 584 AA.
AC A0A367XXD8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=PLB2_2 {ECO:0000313|EMBL:RCK57910.1};
GN ORFNames=Cantr_06884 {ECO:0000313|EMBL:RCK57910.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK57910.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK57910.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK57910.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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:RCK57910.1}.
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DR EMBL; QLNQ01000028; RCK57910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XXD8; -.
DR STRING; 5486.A0A367XXD8; -.
DR Proteomes; UP000253472; 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:UP000253472};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 18..584
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5016483826"
FT DOMAIN 30..547
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 584 AA; 64393 MW; B2AE57A50F955038 CRC64;
MILRLIFISL IVSSVLCKSP TNSYAPGWVT CPNGALTRSS FDGLNPDEKS YIDRRYRLAK
QSLAQFLKDA NMTDLMLTRS WRPGAGELSA LDSRSPNPSV LSGILQSSSY IAGLSGGAWM
VGSIASNDLI TVDQVLAQGS LWDLLNSLFA YNGLLLVLSN TLMWTGIDLL VKLKFLSGST
VSITDIYARA LSYQLLSNYN KKGSAFCWSD VTSLPSFQNS ELPYPILAAV GREPGTSIIN
FNSTVFELTP YEIGSWDPSL RSFMSSQYLG STVDNGVASG RCIQGFDNAG FLMGTSSSLF
NAILLEVNKL NFPEFIKSLI NAIVIDPYER LNVDIAHYNP NPFYKSQNPD GKIANSRTLY
LADGGEDGQN VPLLPLVHRN LSVIFAYDNS ADTDTGWPDG TSLIKTYERQ FSHQGQGVAF
PYVPDQYTFR NLNLTSRPTF FGCDAKNLSS LTDNIYDVPL VIYTGNRPFS YWSNTSTFKL
KYSDSEKQGM VANGYDVASR KDGQVDDEWA ACVGCAIIRR EQERQGIEQS EQCKRCFERY
CWDGTVYQGP PLGDNFDDDG LIPGATYYNS NNLQGIYSGG IALV
//
