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Database: UniProt/TrEMBL
Entry: C5DYG4_ZYGRC
LinkDB: C5DYG4_ZYGRC
Original site: C5DYG4_ZYGRC 
ID   C5DYG4_ZYGRC            Unreviewed;       590 AA.
AC   C5DYG4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=ZYRO0F12826g {ECO:0000313|EMBL:CAR28825.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28825.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000018,
CC         ECO:0000256|RuleBase:RU361171};
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; CU928178; CAR28825.1; -; Genomic_DNA.
DR   RefSeq; XP_002497758.1; XM_002497713.1.
DR   AlphaFoldDB; C5DYG4; -.
DR   STRING; 559307.C5DYG4; -.
DR   GeneID; 8205525; -.
DR   KEGG; zro:ZYRO0F12826g; -.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   InParanoid; C5DYG4; -.
DR   Proteomes; UP000008536; Chromosome F.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
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:UP000008536}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         316
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   590 AA;  66331 MW;  B82B7FEE8CB4E965 CRC64;
     MLYKHTRSQK QPRSLNQRSH PEKGLEDAAL LPEHLSKVSL SNSSQDVDPT LHAPHIHYSV
     PEHGVPEQKA YDLIHNELTL DGNPHLNLAS FVNTESTDLA KKLINENVNK NLADNDEYPQ
     LIELTQRCIS MISQLWKVNE NDEPIGCATT GSSEAIMLGG LAMKKRWEHR MRAAGKPIDK
     PNIIMSSACQ VALEKFARYF EVEAREVPVN AHSHHSLDPK NLWDFVDENT IGIFVILGTT
     YTGHFESVDA TAEVLSQIES QHPEWSNKEI PIHVDGASGG FVVPFAFSDK QMATINNGNW
     GFNNPRVVSM NASGHKFGLT TPGLGWVLWK SEDYLAEELR FKLKYLGGVE ETFGLNFSRP
     GFQVVHQYFN LVSLGKQGYQ DRFNKSLFVA RTFCHALLHN ETFPGAFEPV SSIHQRISDG
     STPQHPQDYW NHPELYTPGV PLVAFKLTSA FHKKYPEIPQ SVISGLLRAR GWIIPNYPLP
     KSTDGSDKQE VLRVVFRSEM SLDLALMLLQ DIEAVLGKAI RSYKAIESSV DQMNSEGAKN
     LIYKMLNSLT TPDSGEDDND DADEGEKKQR REARLGNEHD HVHKNYRGTC
//
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