ID H8X8M4_CANO9 Unreviewed; 575 AA.
AC H8X8M4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=CORT_0F02750 {ECO:0000313|EMBL:CCG24499.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG24499.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG24499.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681724; CCG24499.1; -; Genomic_DNA.
DR RefSeq; XP_003870628.1; XM_003870579.1.
DR AlphaFoldDB; H8X8M4; -.
DR GeneID; 14541457; -.
DR KEGG; cot:CORT_0F02750; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000005018; Chromosome 6.
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}; Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 18..575
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005134665"
FT DOMAIN 28..565
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 575 AA; 63230 MW; 78238CCFA894C0C0 CRC64;
MFFGVLLFLI NAHTIFAKSD GYAPVKVKCP GGKLGRFASP GLNENEIAYM QSRYPIAKKN
LADYLHSAVL DDFEVNSFLD RASPTIGIAF SGGGYRALLT GAGEYAALDA RTHILQGAGL
GGILQSSSYI SGLSGGAWLV GSVVSNDLIS IDELIHNNTL WQTTNSILNY FGDNIVDQLL
MWIDIGEQVR AKQEAGFSIS ITDIWGRALS YQLLTNKKDY GAEYRFSDVM NETNFRNYYA
PFPILLAVGR VPDTTIINLN STVFSFTPFE VGSESPYLNS FVGTGSIGTL LDNGYPQNST
CIKGFDNAGF FMGTSSSLFN AIILSIDNTT LPEFLKDFIN GYILDPIVKS NIDVAKYNPN
PFYQSQGPQT PIEASKTLYL VDGGEDGQNI PLEPLLKRNV SVVFAFDNSA DIDGLPDGTS
MVKTYERQFS IAGENTPFPY VPDQNSFLKL NLTSRPTFLG CNASNLTALT PNIFDVPLII
YIANKPYSFA SNTSTFKLSY SMSNRNSMIT NGFEIASMLN GTLDEEWKAC VGCAIIRREQ
EKMGLEQTKQ CSLCFERYCW NGTIHEEKPS NYTCS
//
