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Database: UniProt
Entry: G8GT15_RALSL
LinkDB: G8GT15_RALSL
Original site: G8GT15_RALSL 
ID   G8GT15_RALSL            Unreviewed;       312 AA.
AC   G8GT15;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Glutamate dehydrogenase oxidoreductase {ECO:0000313|EMBL:AET79775.1};
DE   Flags: Fragment;
GN   Name=gdhA {ECO:0000313|EMBL:AET79775.1};
OS   Ralstonia solanacearum (Pseudomonas solanacearum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=305 {ECO:0000313|EMBL:AET79775.1};
RN   [1] {ECO:0000313|EMBL:AET79775.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BRs-Kal {ECO:0000313|EMBL:AET79775.1};
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; JN180263; AET79775.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8GT15; -.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          118..311
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:AET79775.1"
FT   NON_TER         312
FT                   /evidence="ECO:0000313|EMBL:AET79775.1"
SQ   SEQUENCE   312 AA;  33082 MW;  05991EF24EF5A178 CRC64;
     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 DA
//
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