ID A0A345RHI3_9RHOB Unreviewed; 476 AA.
AC A0A345RHI3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=C1J05_14580 {ECO:0000313|EMBL:AXI57020.1};
OS Sulfitobacter sp. JL08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=2070369 {ECO:0000313|EMBL:AXI57020.1, ECO:0000313|Proteomes:UP000253748};
RN [1] {ECO:0000313|EMBL:AXI57020.1, ECO:0000313|Proteomes:UP000253748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL08 {ECO:0000313|EMBL:AXI57020.1,
RC ECO:0000313|Proteomes:UP000253748};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) 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; CP025815; AXI57020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345RHI3; -.
DR KEGG; suli:C1J05_14580; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000253748; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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: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:UP000253748}.
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; 52476 MW; 9E1A3274DE8D534B CRC64;
MSAKTEPSFR ESVDLMFNRA VALMDLPPGL EEKIRVCNAT YTVRFGVRLR GQIQTFTGYR
SVHSEHMEPV KGGIRYAIGV NQDEVEALAA LMTYKCALVE APFGGSKGGL RINPREYDEH
ELELITRRFA YELAKRDLIH PSQNVPAPDM GTGEREMAWI ADQYKRMNTT DINSAACVTG
KPLNAGGISG RVEATGRGVQ YALQEFFRHP EDIKAAKLSG TLDGKRVIVQ GLGNVGYHAA
KFLSEEDGSV ITGIIERDGA LFNPKGLDVE SVHRWIAKHG GVTGYPDAAH TAEGAAVLEE
DCDILIPAAL EGVINLSNAD RIKANLIIEA ANGPVTAGAD DILREKGVVI IPDMYANAGG
VTVSYFEWVK NLSHIRFGRM QRRQEESRHQ LVVDELERLS ADKQLGWTLS PDFKTKYLRG
AGELELVRSG LDDTMRIAYQ SMREVWHSRE DVDDLRTAAY LVAITKVAAS YRAKGL
//
