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   27-MAR-2024, entry version 118.
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 / NBRC 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 /
RC   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; 284590.O59863; -.
DR   GlyCosmos; O59863; 15 sites, No reported glycans.
DR   PaxDb; 284590-O59863; -.
DR   GeneID; 2892361; -.
DR   KEGG; kla:KLLA0_C05940g; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; O59863; -.
DR   OMA; FGHINMS; -.
DR   BRENDA; 3.1.1.5; 2825.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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
//