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Database: UniProt/TrEMBL
Entry: Q0KEF0_CUPNH
LinkDB: Q0KEF0_CUPNH
Original site: Q0KEF0_CUPNH 
ID   Q0KEF0_CUPNH            Unreviewed;       435 AA.
AC   Q0KEF0;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   Name=gdhA1 {ECO:0000313|EMBL:CAJ91621.1};
GN   OrderedLocusNames=H16_A0471 {ECO:0000313|EMBL:CAJ91621.1};
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ91621.1, ECO:0000313|Proteomes:UP000008210};
RN   [1] {ECO:0000313|EMBL:CAJ91621.1, ECO:0000313|Proteomes:UP000008210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337 {ECO:0000313|Proteomes:UP000008210};
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC       ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; AM260479; CAJ91621.1; -; Genomic_DNA.
DR   RefSeq; WP_010813918.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0KEF0; -.
DR   SMR; Q0KEF0; -.
DR   STRING; 381666.H16_A0471; -.
DR   GeneID; 57642567; -.
DR   KEGG; reh:H16_A0471; -.
DR   PATRIC; fig|381666.6.peg.834; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_2_4; -.
DR   OMA; WLQNRNG; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   Gene3D; 1.10.8.1210; -; 2.
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; IPR014362; Glu_DH.
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   PIRSF; PIRSF000185; Glu_DH; 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   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008210}.
FT   DOMAIN          203..432
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         210
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            166
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   435 AA;  47333 MW;  11DD8D06A70F6F83 CRC64;
     MSSAAPTNIA GQKHALPSYL NADHLGPWGI YLQQVDRVTP YLGSLARWVE TLKRPKRAMI
     VDVPIELDNG TIAHFEGYRV QHNLSRGPGK GGVRFHQDVT LSEVMALSAW MSVKNAAVNV
     PYGGAKGGIR VDPRTLSHAE LERLTRRYTS EINIIIGPSK DIPAPDVNTN AQVMAWMMDT
     YSMNSGSTAT GVVTGKPISL GGSLGRHEAT GRGVFVVGSE AARNIGLEIK GARVAVQGFG
     NVGAVAAKLF HEAGAKVVAV QDHRTTLFDP AGLDVPAMME YASHSGTIEG FRGEVLRTEQ
     FWEVDCDILI PAALEGQITV QNAPKITAKL VIEGANGPTT PQADDILRER NILVCPDVIA
     NAGGVTVSYF EWVQDFSSFF WTEEEINQRL VRIMQEAFRA IWQVAQDNKV TLRTAAFIVA
     CTRILQAREM RGLYP
//
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