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Database: UniProt
Entry: G8GT25_RALSL
LinkDB: G8GT25_RALSL
Original site: G8GT25_RALSL 
ID   G8GT25_RALSL            Unreviewed;       331 AA.
AC   G8GT25;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Glutamate dehydrogenase oxidoreductase {ECO:0000313|EMBL:AET79785.1};
DE   Flags: Fragment;
GN   Name=gdhA {ECO:0000313|EMBL:AET79785.1};
OS   Ralstonia solanacearum (Pseudomonas solanacearum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=305 {ECO:0000313|EMBL:AET79785.1};
RN   [1] {ECO:0000313|EMBL:AET79785.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GRs-Pul {ECO:0000313|EMBL:AET79785.1};
RA   Kumar A., Prameela T.P.II., Bhai S.R.;
RT   "Multilocus sequence typing of Ralstonia solanacaearum causing bacterial
RT   wilt of ginger in India.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; JN180273; AET79785.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8GT25; -.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          128..329
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AET79785.1"
FT   NON_TER         331
FT                   /evidence="ECO:0000313|EMBL:AET79785.1"
SQ   SEQUENCE   331 AA;  35410 MW;  FF0F9C7A8D1B20EB CRC64;
     ESYRVQHNTS RGPGKGGVRF HQDVTLSEVM ALSAWMSVKN AAVNVPYGGA KGGVRVDPRK
     LSSGELERLT RRYTSEIGII IGPNKDIPAP DVNTNAQIMA WMMDTYSMNE GATATGVVTG
     KPIALGGSLG RREATGRGVF VVGSEAARNL GIDVKGARIV VQGFGNVGSV AAKLFQDAGA
     KVIAVQDHKG IVFNGAGLDV DALIQHVDHN GSVDGFKAET LSADDFWALE CEFLIPAALE
     GQITGKNAPQ IKAKIVVEGA NGPTTPEADD ILRDRGILVC PDVIANAGGV TVSYFEWVQD
     FSSFFWTEDE INQRLVRIMQ DAFRAIWQVP Q
//
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