ID   C4XZE9_CLAL4            Unreviewed;       527 AA.
AC   C4XZE9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CLUG_01331 {ECO:0000313|EMBL:EEQ37208.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ37208.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ37208.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ37208.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CH408077; EEQ37208.1; -; Genomic_DNA.
DR   RefSeq; XP_002617872.1; XM_002617826.1.
DR   AlphaFoldDB; C4XZE9; -.
DR   STRING; 306902.C4XZE9; -.
DR   GeneID; 8499483; -.
DR   KEGG; clu:CLUG_01331; -.
DR   VEuPathDB; FungiDB:CLUG_01331; -.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; C4XZE9; -.
DR   OMA; AGMVIFK; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT   MOD_RES         337
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   527 AA;  59170 MW;  03F5A0A25D8480C0 CRC64;
     MKTFKPRPSF SDPTVYYSLS QVSFPMISSD LETDRVQELD QLLSLIHPRI VDYVASADAN
     SEKFQANSLG SFHEPSELKK IFTSEEGIFE RGLKNDHDSL FHHIDNVLKY SVNTWNPGFL
     DKLYASNNPI GVISDIILSV LNTNSHVYTV SPVLSVLENY MGRKYARLFY SNHQDTCGGL
     TFSGGSWSNI TAMQIARSIK YPETKLHGNG NFKFAVYASK HCHYSIEKAA ILLGIGSKSV
     FKVDINSDGT MNTRSLEETI QKSISEGYTP LFINTTAGTT VFGSYDDIQA ASAIAKKFNV
     WLHVDGSWGG NVIFSEVHKK KLKGSEFADS ITTNPHKMLG TPNTCSFLLL PDVKTFQTAN
     SLAAPYLFHG RENDEENMDL ADGTMGCGRR ADAFKFYLTW LYYGYDGLQQ RVDHAFRIVE
     YFVQSITNVP GFTLVDEHPQ CLQVCFYYRP EGYEGDDMTN ITRFISRTLH SQGRYLMDFS
     PNPTKDEKGE FFRVVFNSPI LTDKIIDDLV ASIVSVGAAY QNKMGQS
//