ID A5DDD7_PICGU Unreviewed; 666 AA.
AC A5DDD7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=PGUG_01288 {ECO:0000313|EMBL:EDK37190.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK37190.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK37190.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408156; EDK37190.2; -; Genomic_DNA.
DR RefSeq; XP_001485617.1; XM_001485567.1.
DR AlphaFoldDB; A5DDD7; -.
DR STRING; 294746.A5DDD7; -.
DR GeneID; 5127654; -.
DR KEGG; pgu:PGUG_01288; -.
DR VEuPathDB; FungiDB:PGUG_01288; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_1_1; -.
DR InParanoid; A5DDD7; -.
DR OMA; SWWKANE; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000001997; 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 CDD; cd07203; cPLA2_Fungal_PLB; 1.
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:UP000001997};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 20..666
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005121636"
FT DOMAIN 53..605
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 73488 MW; FE6A15106BF73FEE CRC64;
MLILGYLWYI YLLVFPVAAF DWPWEDDSSS ASGSASATET DSDRNKYAPY ETDCPSGELT
RQSVNISDGE RDYITHRWEK TNNKLIEFLS ERANLSDFDA ETYINDYSDE HNITIGVAFS
GGGYRAMLCG AGELLGLDDR YDGEDSENGL GGLLQSSTYI AGLSGGNWLV GSMVLNDWIS
VADIYSGKKK IWDLEDSIFN PNGINVIKTV EYYKHIYDAL NAKKDAGFET SITDIWGRAL
SNQFFEGDQG GENVTWSSIQ DLSSFKDYEM PFPVVVADGR TPGTYIINSN STVFEFNPFE
MGSWDPSVHT FFDVKYLGSG VSGGDPKNDK CTANFDNAGF VLGTSSSLFN QVILRLPGTS
IPSVLKSLLN KLLKSVSNDE DDIAVYEPNP FYDSEYGGSR SVLKNDTLYL CDGGEDNQNV
PLYPLIQTVR KLDIILAYDN SADTNQNWPN GSSLVETYQR QYSVQGRGTP FPYVPSVDEF
VDKELNKRPV FFGCDASNMT DLVQQSKNNN INETDIPLVV YMPNHRHSYN SNTSTYKMSY
DNDEKWGVIR NGFEVTTQKN GTTDDGWATC MGCAIIRRSQ ERRGIKQSSE CEKCFQKYCW
NGGSKDAVAS TDAASPTGSS SSSSSKSSSQ SSSTSTGKKK GAATSVSAPW QAVVYVVLLI
SGAFII
//
