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Database: UniProt
Entry: M3JYB4_CANMX
LinkDB: M3JYB4_CANMX
Original site: M3JYB4_CANMX 
ID   M3JYB4_CANMX            Unreviewed;       699 AA.
AC   M3JYB4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=G210_1558 {ECO:0000313|EMBL:EMG47970.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47970.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG47970.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) 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:EMG47970.1}.
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DR   EMBL; AOGT01001322; EMG47970.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3JYB4; -.
DR   STRING; 1245528.M3JYB4; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_2_0_1; -.
DR   OMA; FIANCRN; -.
DR   OrthoDB; 1980513at2759; -.
DR   Proteomes; UP000011777; 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:SF56; MEIOTIC PHOSPHOLIPASE SPO1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 2.
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:UP000011777};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           21..699
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005140327"
FT   DOMAIN          47..699
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   699 AA;  79746 MW;  3082963BB4346F3C CRC64;
     MLILTLVFPC VVWCIIYTDT NKLLCKNSSN IVDRPPWNLS YAPFTITCPK GKLIRQANEK
     LCNEEYEYIS NRNKKTELSL ESLFYRNKIP HFDVCNFWSI KAKPTRIAIA ISGGGYRSMI
     TSGGILLSFD NRYSQSNLLG GLLQSTSYIA GISGGAWLVL SNFINDFECV DKLVHGGWNF
     EDPLLLGVPK FEPDEMINKQ NTSGIFQLVL NWFKTDDDKK KDTNKFWLTN WISQFFGTKL
     INYYYTNEQA ELDTFISIKK YLTFYKELLI EVKDKKKAGF HTSFTDYFGR ALVRKIFKAT
     ARTPGTTITA ATRALPSFLE YDQPFPIACT IEKDPSIPGF SSHLDSHCFE FTPYEFGSWD
     SYLNAFVPMK YLGTTFQNGE SVNKSTNFSY CVSGFDNVGF VTGTSSSLFN HVFLIIHQML
     ESYQSETTTT IKSILKALGL SSEWNGLKLP NLHPDYALYS PNPFYQYGTT NISNNSDLYL
     VDGGDDGQNI PFHPFLNAAR EVDIIFAYDM TNERDNYPNG TVLARTSQRY KQTNNSNIQI
     PYFEIPQGDS IQEKIIKSIF PKVPTPEQII QQELTKNPIF LGCDIIEDYE TLEVVNPNQV
     RPIGYLPPLI IYHANNEYSY ASNTSTFQLS YNQTEVYGMI NNGFNLATNN NSTIFSICMN
     CAILKREFDR ISYGLNTKSD GFVVPKICQK CYKTFCWRD
//
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