ID A0A1G4IS73_9SACH Unreviewed; 643 AA.
AC A0A1G4IS73;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=LANO_0A06238G {ECO:0000313|EMBL:SCU79434.1};
OS Lachancea nothofagi CBS 11611.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU79434.1};
RN [1] {ECO:0000313|EMBL:SCU79434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ploux O.;
RL Submitted (MAR-2016) 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}.
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DR EMBL; LT598449; SCU79434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4IS73; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000189911; Chromosome a.
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}; Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 18..643
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5009028878"
FT DOMAIN 30..579
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 643 AA; 69807 MW; 646A03DF53D2D577 CRC64;
MFWLLGALAL VLNAVIAWSP TNGYAPGNVS CDDNINLVRE ATGLSANETA WLEKRDAYTK
DSLKDFLDRA TANFTNSSFV DSLWNTGKIP KLGVGCSGGG YRAMLSGAGM LSALDNRTDG
ANEHGLGGVL QAATYLAGLS GGNWLVGSLA WNNWTSVQQV IDNRGQDDEL WDISNSLLNP
GGINILSSAS RWDQISDAVE AKQDAGFNAS LTDVWGRALS YEFFPTLYRG GEGYTWSTLR
DSDVFKNAEM PFPISVADGR YPGTQIVDLN STVFEFNPFE MGSWDPSLNA FTDVKYLGTN
VTNGTPVTQG KCVAGFDNAG FIMGTSSSLF NQFLLQLNTT GLSSFIKGFV GDFLQDLSND
SDDIAIYNPN PFKDTHFVSS NHSQSIVTAE NLYLVDGGED GENIPFLPLL QKDRDLDVIF
ALDNSADTDQ YWPAGLSLIS TYERQFGSLG KDLAFPYVPD VDTFVNSGLN TKPTFFGCDA
TNLTGLAYTP PLIVYMPNNR QSYNSNTSTF KMSYSSDQRM KMFQNGFEAI TRNNLTDDSA
FTGCVACAIM KRKQESLNMT LPEECTQCFK DYCWDGKLAT KSSNVTTLGT YSGSISFVTD
SASSSSTASS TSKKNNAVAL SQSYSMNWYV AFAAILGVTL GLL
//
