ID A6ZM68_YEAS7 Unreviewed; 706 AA.
AC A6ZM68;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=PLB2 {ECO:0000313|EMBL:EDN64398.1};
GN ORFNames=SCY_4180 {ECO:0000313|EMBL:EDN64398.1};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN64398.1, ECO:0000313|Proteomes:UP000007060};
RN [1] {ECO:0000313|EMBL:EDN64398.1, ECO:0000313|Proteomes:UP000007060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN64398.1,
RC ECO:0000313|Proteomes:UP000007060};
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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:EDN64398.1}.
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DR EMBL; AAFW02000020; EDN64398.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZM68; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR Proteomes; UP000007060; 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}; Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 20..706
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005121761"
FT DOMAIN 36..588
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 627..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 75481 MW; 1A7686287F0D05BB CRC64;
MQLRNILQAS SLISGLSLAA DSSSTTGDGY APSIIPCPSD DTSLVRNASG LSTAETDWLK
KRDAYTKEAL HSFLSRATSN FSDTSLLSTL FSSNSSNVPK IGIACSGGGY RAMLGGAGMI
AAMDNRTDGA NEHGLGGLLQ SSTYLSGLSG GNWLTGTLAW NNWTSVQEIV DHMSESDSIW
NITKSIVNPG GSNLTYTIER WESIVQEVQA KSDAGFNISL SDLWARALSY NFFPSLPDAG
SALTWSSLRD VDVFKNGEMP LPITVADGRY PGTTVINLNA TLFEFTPFEM GSWDPSLNAF
TDVKYLGTNV TNGKPVNKDQ CVSGYDNAGF VIATSASLFN EFSLEASTST YYKMINSFAN
KYVNNLSQDD DDIAIYAPNP FKDTEFVDRN YTSSIVDADD LFLVDGGEDG QNLPLVPLIK
KERDLDVVFA LDISDNTDES WPSGVCMTNT YERQYSKQGK GMAFPYVPDV NTFLNLGLTN
KPTFFGCDAK NLTDLEYIPP LVVYIPNTKH SFNGNQSTLK MNYNVTERLG MIRNGFEAAT
MGNFTDDSNF LGCIGCAIIR RKQESLNATL PPECTKCFAD YCWNGTLSTS ANPELSGNST
YQSGAIASAI SEATDGIPIT ALLGSSTSGN TTSNSTTSTS SNVTSNSNSS SNTTLNSNSS
SSSISSSTAR SSSSTANKAN AAAISYANTN TLMSLLGAIT ALFGLI
//
