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
//