ID   C5M9P0_CANTT            Unreviewed;       485 AA.
AC   C5M9P0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CTRG_02202 {ECO:0000313|EMBL:EER33384.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER33384.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER33384.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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; GG692397; EER33384.1; -; Genomic_DNA.
DR   RefSeq; XP_002547905.1; XM_002547859.1.
DR   AlphaFoldDB; C5M9P0; -.
DR   STRING; 294747.C5M9P0; -.
DR   EnsemblFungi; CTRG_02202-t43_1; CTRG_02202-t43_1-p1; CTRG_02202.
DR   GeneID; 8296903; -.
DR   KEGG; ctp:CTRG_02202; -.
DR   VEuPathDB; FungiDB:CTRG_02202; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000002037; 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:UP000002037}.
FT   MOD_RES         300
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   485 AA;  54620 MW;  C868F6A449FF25ED CRC64;
     MNTAEELDKL LTELKPRLLA YIDEADPKSS NYNPQSLGTF HEPKFLKQEF IQDDNLDEPC
     SETKLFEIID KVLKYSVNTW NPGFLDKLYA SNNPIGVISD ILLSMLNTNS HVYTVSPVLS
     VLENYIGKKY ASLFYENETC GGLTFSGGSW SNITSLQLAR SLKYPDTKTK GNAGYKFAIY
     SSKHSHYSVE KAAILLGLGA ENVFKVNVDE DGVMDVQELE AIIEKTKADG YTPLYVNATA
     GTTVFGSYDP FVEISKIAKK HNIHFHIDGS WGGNVIFSEK YKNRLNGCQY ADSITVNPHK
     MLGIPNTCSF LLLPDVSNFQ TAMSLKAPYL FHGRESGDDE NYDLADGTMG CGRRSDAFKF
     YLGWLYYGKE GFAKRVDHAY KIMEYFVDKI KSNDDFKVVG PQSPQCLQVC FYYHPPSVST
     RDNTEITRFI SRKLHKLGKY LVDFSPNPVD DSQGEFFRVV FNSPTLTNEI IDDLINSIIE
     VGKEL
//