ID A0A2R8AKH7_9RHOB Unreviewed; 476 AA.
AC A0A2R8AKH7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA {ECO:0000313|EMBL:SPF76543.1};
GN ORFNames=ALP8811_01551 {ECO:0000313|EMBL:SPF76543.1};
OS Aliiroseovarius pelagivivens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1639690 {ECO:0000313|EMBL:SPF76543.1, ECO:0000313|Proteomes:UP000244911};
RN [1] {ECO:0000313|EMBL:SPF76543.1, ECO:0000313|Proteomes:UP000244911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8811 {ECO:0000313|EMBL:SPF76543.1,
RC ECO:0000313|Proteomes:UP000244911};
RA Keele B.F.;
RL Submitted (MAR-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; OMOI01000001; SPF76543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AKH7; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000244911; 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:UP000244911}.
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; 52912 MW; 9E9EAACFF9491EC4 CRC64;
MSLTNEPSFR ESVELMFNRA ASLMNLPSGL EEKIRVCNAT YTVRFGVRLR GEIKTFTGYR
SVHSEHMEPV KGGIRYAISV DQDEVEALAS LMTFKCALVE TPFGGSKGGL CIDPREYEEH
ELELITRRFA YELAKRDLIN PSQNVPAPDM GTGEREMAWI ADQYARMNTT DINARACVTG
KPPHAGGIAG RVEATGRGVQ YALREFFRHP EDIKLANLSG KLKDKRIIVQ GLGNVGYHAA
KFLSHEDGSR IIGVIERDGA LYDANGLDVE AVHQWIAGHG GVKGFADAQF VENGADLLEV
ECDILIPAAL EGVINLTNAE RIKAPLIIEA ANGPITSGAD KVLRDKGVVI IPDLYANAGG
VTVSYFEWVK NLSHIRFGRM QRRQEEARHQ LVVDELERLD RYLGDAWSMS PAFKEKYLRG
ADELELVRSG LDDTMRVAYQ SMREVWHSRD DVDDLRMAAF IVAIERIAAS YRAKGL
//