ID G8YSP8_PICSO Unreviewed; 783 AA.
AC G8YSP8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=Piso0_000556 {ECO:0000313|EMBL:CCE73510.1};
GN ORFNames=GNLVRS01_PISO0A11946g {ECO:0000313|EMBL:CCE72949.1},
GN GNLVRS01_PISO0B12013g {ECO:0000313|EMBL:CCE73510.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE73510.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|EMBL:CCE73510.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 7064 {ECO:0000313|EMBL:CCE73510.1};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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; FO082059; CCE72949.1; -; Genomic_DNA.
DR EMBL; FO082058; CCE73510.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YSP8; -.
DR STRING; 559304.G8YSP8; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; G8YSP8; -.
DR OMA; FIANCRN; -.
DR Proteomes; UP000005222; Chromosome A.
DR Proteomes; UP000005222; Chromosome B.
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; 2.
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:UP000005222};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 18..783
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5007362039"
FT DOMAIN 72..773
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 783 AA; 87764 MW; 63262268B0C52182 CRC64;
MIILLYMLFV LKGFVVCRPL LFGPAQKLQM KGYTRRETRV VNSLDLISSE NTDIFGSNQY
YWRSSYAPYK TLCPSYNLLR AANNDISKEE SRYIKHRRDL AMVALQELLE RNRIPGFDAN
EFLDKYSKYV TIALAFSGGG YRSMLTGGGA LVAYDSRTPG TESEGQLGGL FQASSYIGGI
SGGSWLVMSN LVNDNRPIIE LKDDPKAWSL QHKLLEGVPN FDPTSIQKTQ SDQSSLVPNN
NGYIFDNNDI ETKEKNPFAA FFSKIFHFAK IFPYEKEDTP LDQKEQPILT SSVLDLLKSI
LLKNDEDHDN STGKSPENTV WKRVFSYYKE LNIEVRSKRS AGYYVSFTDY WGRALARRIF
PGVARIPGVT ITESTFLPSF KNYEQPFPVI GTIEKTPSKT SSSIDSHLFE FTPYEFGSWD
DYLGAFVPLR YLGSSLYDGV PIQPTKISNI SICVSGYDNV GYMTGASSCL FSHIFVYIYN
FLVSFKSELS VAANSLLTSF GLSAGTTSLN NPQYHPDYAL ISPNPFYGFK PIKDTYKGLS
ESSHMYLVDG GDDGQNIPFQ PFIQPAREVD IIFAFDMTSD HNNFPNGTTL RKSTERYHSN
ATEFSVPYFE HIYQGKGQRE PTLTQRSAFP SVPTPEDIVC YNLSSSPIFL GCDLDDFPPV
NVTALSPTGG KTSGYIPPLI IYTANSALTS QSNTSTFQLS YSPYEVNKMI ENGYSLATNG
NSTSYSTCVS CAILKRQFDH IATNRANSYN DSFKIPNACK ACFQQYCWKG KYSKARSHKA
DLN
//
