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Database: UniProt
Entry: A0A2R8AKH7_9RHOB
LinkDB: A0A2R8AKH7_9RHOB
Original site: A0A2R8AKH7_9RHOB 
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
//
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