ID   G8ZNN1_TORDE            Unreviewed;       579 AA.
AC   G8ZNN1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   Name=TDEL0B00960 {ECO:0000313|EMBL:CCE90225.1};
GN   ORFNames=TDEL_0B00960 {ECO:0000313|EMBL:CCE90225.1};
OS   Torulaspora delbrueckii (Yeast) (Candida colliculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Torulaspora.
OX   NCBI_TaxID=4950 {ECO:0000313|EMBL:CCE90225.1, ECO:0000313|Proteomes:UP000005627};
RN   [1] {ECO:0000313|EMBL:CCE90225.1, ECO:0000313|Proteomes:UP000005627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866
RC   {ECO:0000313|Proteomes:UP000005627};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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|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; HE616743; CCE90225.1; -; Genomic_DNA.
DR   RefSeq; XP_003679436.1; XM_003679388.1.
DR   AlphaFoldDB; G8ZNN1; -.
DR   STRING; 1076872.G8ZNN1; -.
DR   GeneID; 11503435; -.
DR   KEGG; tdl:TDEL_0B00960; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   InParanoid; G8ZNN1; -.
DR   Proteomes; UP000005627; Chromosome 2.
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:UP000005627}.
FT   REGION          557..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         320
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   579 AA;  65735 MW;  25894D43B70801CB CRC64;
     MLHKHSDRQK RPRTLVQHHH MDSYKGLEEA NLLPQQVQGL HLGTATKAEE HEGNHILSNR
     YKIPQRGIGE QTAYDLIHNE LTLDGNPHLN LASFVNTDAS DIARRLISEN MLKNLADNDE
     YPQLIEITQR CISMLAQLWK CDNEKDDPIG CATTGSSEAI MLGGLAMKKR WEHRMQDAGK
     SIAKPNIVMS SACQVALEKF ARYFEVECRL IPVSTKSHSC LDPKMLWDYV DENTIGAFVI
     LGTTYTGTLE NVEQVSEVLT EIENANPKWS NKDIPIHVDG ASGGFVVPFA FEEAQLAEYK
     MSRWGFNHPR VMSINTSGHK FGLTTPGLGW VLWKDESLLA SELKFKLKYL GGVEETFGLN
     FSRPGFQVIH QYYNLVTLGH QGFHSHFNKS LFVARAFCHE LLASPRMPNM FEVVSCIHER
     IADDKLPESV NDYWENPAHF KPGVPLAAFK LSREFHEKYP EIPQSMLSSM LRNRGWIIPN
     YPLPKSTDDS DQHEVLRVVF RTEMKLDLAQ LLLLDIERAV TKLLDSYKAV TESLANKGAD
     ENREFVYKML LTLASPSDDS APPEHKHRKS FSKNYRGTC
//