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Database: UniProt
Entry: B6BA15_9RHOB
LinkDB: B6BA15_9RHOB
Original site: B6BA15_9RHOB 
ID   B6BA15_9RHOB            Unreviewed;       476 AA.
AC   B6BA15;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=RBY4I_1489 {ECO:0000313|EMBL:EDZ46277.1};
OS   Rhodobacterales bacterium Y4I.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ46277.1, ECO:0000313|Proteomes:UP000005133};
RN   [1] {ECO:0000313|EMBL:EDZ46277.1, ECO:0000313|Proteomes:UP000005133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4I {ECO:0000313|EMBL:EDZ46277.1,
RC   ECO:0000313|Proteomes:UP000005133};
RA   Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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; DS995281; EDZ46277.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6BA15; -.
DR   STRING; 439496.RBY4I_1489; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_0_5; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000005133; Unassembled WGS sequence.
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: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; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
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:UP000005133}.
FT   DOMAIN          188..475
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            149
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   476 AA;  52779 MW;  5E756B897CDB5A75 CRC64;
     MSSRTEPSFR ESVDLMFNRA VSLMDLPPGL EEKIRVCNAT YTVRFGVRLR GAMHTFTGYR
     SVHSEHMEPV KGGIRYAPGV NQDEVEALAA LMTYKCALVE APFGGSKGGL CIDPREYDEH
     ELELITRRFA YELAKRDLIN PSQNVPAPDM GTGEREMAWI ADQYARMNTT DINAKACVTG
     KPLNAGGISG RVEATGRGVQ YALREFFRYE EDKAAAGLTG KLEGKRIIVQ GLGNVGYHAA
     KFLSEEDGAL ITGIIERDGG LYSADGLDVE AVRNWIVKHD GVAGYPDAQF VQDGALLLEE
     ECDVLIPAAL EAVINLENAE RVKAPLIIEA ANGPVTAGAD EILRKKGTVI IPDMYANAGG
     VTVSYFEWVK NLSHIRFGRM QRRQEEARHQ LVIDELQRLD DVMGDTWSMS PHFKEKYLRG
     ADELELVRSG LDDTMRVAYQ SMREVWHSRD DVTDLRTAAY LVSIDKVAKS YHAKGL
//
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