ID   A0A2N4YDQ3_9RHOB        Unreviewed;       475 AA.
AC   A0A2N4YDQ3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=C0V75_17720 {ECO:0000313|EMBL:PLL11300.1};
OS   Tabrizicola sp. TH137.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tabrizicola.
OX   NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL11300.1, ECO:0000313|Proteomes:UP000234539};
RN   [1] {ECO:0000313|EMBL:PLL11300.1, ECO:0000313|Proteomes:UP000234539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH137 {ECO:0000313|EMBL:PLL11300.1,
RC   ECO:0000313|Proteomes:UP000234539};
RA   Cai h.;
RT   "genomes of bacteria within cyanobacterial aggregates.";
RL   Submitted (DEC-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLL11300.1}.
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DR   EMBL; PKRQ01000006; PLL11300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N4YDQ3; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000234539; Unassembled WGS sequence.
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:UP000234539}.
FT   DOMAIN          187..474
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            148
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   475 AA;  51926 MW;  1459A5B2586FF250 CRC64;
     MRAGEPSFRD SVDLMFNRAV RLMDLSPGLE NKIRVCNSTY TVRFGVRLRG KIETFTGYRS
     VHSEHMEPVK GGIRYALSVS QDEVEALAAL MTYKCALVET PFGGSKGGLC IDPRQWDEHE
     LEQITRRFAY ELIKRDLIHP AQNVPAPDMG TGEREMAWIA DQYARMNTTD INAKACVTGK
     PPHAGGIQGR VEATGRGVQF ALREFFRHPE DVAAAGLSGA LEGKRAVVQG LGNVGYHAAK
     FLSEEDGVII TAIIERDGAL ISDAGLEVEA VRQHLTATGG LKGFAGAEYV ADGAKVLEKA
     CDILIPAAME GVIHQGNAAR INAPLIIEAA NGPITFGADE ILRQKGAVII PDMYANAGGV
     TVSYFEWVKN LSHIRFGRMQ RRAEEARSRL MVEELERLSA DKGLGWTLSP DFKEKFLTGS
     DELALVRSGL DDTMRSAYAA MREVWHGRGD VDDLRTAAYI VSIGRVAQTY RSKGL
//