ID C5DTC0_ZYGRC Unreviewed; 632 AA.
AC C5DTC0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN OrderedLocusNames=ZYRO0C07238g {ECO:0000313|EMBL:CAR27031.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR27031.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(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; CU928175; CAR27031.1; -; Genomic_DNA.
DR RefSeq; XP_002495964.1; XM_002495919.1.
DR AlphaFoldDB; C5DTC0; -.
DR STRING; 559307.C5DTC0; -.
DR GeneID; 8203171; -.
DR KEGG; zro:ZYRO0C07238g; -.
DR HOGENOM; CLU_014602_0_1_1; -.
DR InParanoid; C5DTC0; -.
DR Proteomes; UP000008536; Chromosome C.
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:UP000008536};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 19..632
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005125155"
FT DOMAIN 31..581
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 590..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 69325 MW; 7F0532AD526F5E87 CRC64;
MNFIESLLVL VVAGLAAAWS PKNSYVPSTV NCPDDIVLVR EANGLSDNET EWLKRRRPIA
KEALHDFVKR ATKNFSDNSL VDKVFSGNDS HAPVVAIGAS GGGYRAMLSG AGMISAFDNR
TRGADEHGLG GVLQGATYLA GLSGGNWLTG TLAWNNWTSV QTIVDNTTAD DSIWDISHSL
VNPDGVNVFG TADHWEHIFK TVRQKHKTYN ASLTDLWGRA LSYDFFPSLY RGGEAYTWST
LRDAEVFENG SMPFPISVAD GRYPGTSVIS LNATVFEFNP FEMGSWDPSL RAFTDVKYLG
TKAVDGKPEK KGECVAGYDN VGFIMGTSST LFNQFLLRLN TTGMPRVVKS IISHFLKDIS
KNEDDIAVYS PNPFLNTSYV SNDYTSSLVD SKDLYLVDGG EDNENIPLLP FLQKERGVDV
IFALDNSADT TEYWPDGSSL VATYERQFGK MGKDIAFPYV PDVETFVAEG LNTKPTFFGC
DAQNMSDLAF TPPLVVYVPN SRMSYNGNQS TFKLSYSDNE RLNMIKNGFE ATTRNNLTDD
SNFAGCVACA IMRRSQESMN ATLPKECKQC FQDYCWNGHI SHNGTKIQHN DDYTKSASPS
ATSSSKGGAS NSYSPRSGLS LFAFMVTVAG LF
//
