ID   G0JR49_9PROT            Unreviewed;       457 AA.
AC   G0JR49;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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   ORFNames=Acife_2615 {ECO:0000313|EMBL:AEM48695.1};
OS   Acidithiobacillus ferrivorans SS3.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM48695.1, ECO:0000313|Proteomes:UP000009220};
RN   [1] {ECO:0000313|EMBL:AEM48695.1, ECO:0000313|Proteomes:UP000009220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3 {ECO:0000313|EMBL:AEM48695.1,
RC   ECO:0000313|Proteomes:UP000009220};
RX   PubMed=21705598; DOI=10.1128/JB.05373-11;
RA   Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT   "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT   ferrivorans SS3.";
RL   J. Bacteriol. 193:4304-4305(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|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; CP002985; AEM48695.1; -; Genomic_DNA.
DR   RefSeq; WP_014029944.1; NC_015942.1.
DR   AlphaFoldDB; G0JR49; -.
DR   STRING; 743299.Acife_2615; -.
DR   KEGG; afi:Acife_2615; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_6; -.
DR   Proteomes; UP000009220; Chromosome.
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   CDD; cd06450; DOPA_deC_like; 1.
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:UP000009220}.
FT   MOD_RES         272
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   457 AA;  51813 MW;  20CC50680B798F11 CRC64;
     MVKRFTKDSD LTPAYGSRTM DHTISKYRLP DDEMPAQTAY QLIHDELMLD GNARLNLATF
     VTTWMEPEAE KLMAETFDKN MIDKDEYPQT AEIETRCVNM LARLFNAHPD EHPVGVSAIG
     SSEAVMLAGM ALKWNWRKRR EKAGASAATP NLVMGRSVQV VWEKFCRYWE VEPRYIPMHE
     DRYTLKSEEV LALVDENTIG VVTVLGTTFT GEFDPIAEIH DALVVHNQKT GLQVPIHVDA
     ASGGFVAPFL QPNLLWDFRL PNVVSINTSG HKYGLVYPGV GWALWRGEAH LPEELVFHVN
     YLGGDMPTFT LNFSRPGNQI IGQYYNLLRL GRAGYTRIMR NLRDTALWLS RSIARMGPFV
     LLSDGSSIPV FAMRLKDSSR FTVFDLSRQL RMRGWQVPAY TLPEDATELA VLRLVIREGF
     SRDMADLLLK DLKQAVTDLE QTPPAQKSQD DGHFHHN
//