PLB_KLULA
ID PLB_KLULA Reviewed; 640 AA.
AC O59863;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Lysophospholipase;
DE EC=3.1.1.5;
DE AltName: Full=KlPLB;
DE AltName: Full=Phospholipase B;
DE Flags: Precursor;
GN Name=PLB; OrderedLocusNames=KLLA0C05940g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND MUTAGENESIS OF ARG-112
RP AND ASP-406.
RC STRAIN=ATCC 56498 / CBS 683 / DSM 4394 / IFO 1090 / NRRL Y-8279;
RX PubMed=10052126; DOI=10.1271/bbb.63.83;
RA Oishi H., Morimoto T., Watanabe Y., Tamai Y.;
RT "Purification and characterization of phospholipase B from Kluyveromyces
RT lactis, and cloning of phospholipase B gene.";
RL Biosci. Biotechnol. Biochem. 63:83-90(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC At acidic pH the enzyme hydrolyzes all phospholipid substrates without
CC metal ion. On the other hand, at alkaline pH the enzyme shows substrate
CC specificity for phosphatidylcholine and lysophosphatidylcholine and
CC requires Ca(2+), Fe(3+), or Al(3+) for the activity.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 2.0 and 7.5.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Highly glycosylated.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; AB014495; BAA28619.1; -; mRNA.
DR EMBL; CR382123; CAH01313.1; -; Genomic_DNA.
DR RefSeq; XP_452462.1; XM_452462.1.
DR AlphaFoldDB; O59863; -.
DR SMR; O59863; -.
DR STRING; 28985.XP_452462.1; -.
DR EnsemblFungi; CAH01313; CAH01313; KLLA0_C05940g.
DR GeneID; 2892361; -.
DR KEGG; kla:KLLA0_C05940g; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; O59863; -.
DR OMA; WDISHSI; -.
DR BRENDA; 3.1.1.5; 2825.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
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:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:EnsemblFungi.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..640
FT /note="Lysophospholipase"
FT /id="PRO_0000024637"
FT DOMAIN 38..589
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 594..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 112
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10052126"
FT MUTAGEN 406
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10052126"
SQ SEQUENCE 640 AA; 69983 MW; 90A696CB5D7FF9E3 CRC64;
MWFLNSVNLL FLVCSVALHL DAVNAWSPTN GYAPGVVDCD ENINLVRKAD AVSDDEADWL
KVRHESTVPA LKDFLQRGFK GFTNDTSIID KLLATQDTAP KVAIACSGGG YRAMLSGAGM
ISAMDNRTDG ANDHGLGGLL QSSTYLAGLS GGNWLVGTLA YNNWTSVQAI INNMTDDNSI
WDISNSIVNP GGINIFSSIS RWDDISDAVE EKKKAGFNTS ITDVWGRALS YNFFPSLDEG
GVGYTWNTLR DVDVFKNGEM PFPISVAVGR YPGTQVVNLN ATVFEFNPFE MGSWDYTLHT
FTDVRYAGTN VTNGTPNVTG KCVAGFDNTG FVMGTSSSLF NQFLLQLNTT DLPSFLYNLL
HGFLTDASDD YDDISIWAPN PFYEITNIPS NYSQSISEDD TLYLVDGGED GQNIPLTPLL
QTEREIDVIF ALDNSADTDQ SWPDGFSLTQ TYARQFGLQG KGIAFPYVPD VNTFTNLGLN
TRPTFFGCDA RNLTDLESIP PLVVYMPNTR ESFNSNTSTF KMSYSTSERF KMIQNGFEAV
TMKNLTKDEN FMGCISCAIL RRKQESLNYT LPSECDACFE KYCWNGTVDA TTPISSTTSS
SASSTSTSDS GNKENSARIL APRSTLSLLI GGLASVFISF
