ID   A0A399J5F0_9RHOB        Unreviewed;       476 AA.
AC   A0A399J5F0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=DL237_08455 {ECO:0000313|EMBL:RII39172.1};
OS   Pseudooceanicola sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=2211117 {ECO:0000313|EMBL:RII39172.1, ECO:0000313|Proteomes:UP000265848};
RN   [1] {ECO:0000313|EMBL:RII39172.1, ECO:0000313|Proteomes:UP000265848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CY03 {ECO:0000313|EMBL:RII39172.1,
RC   ECO:0000313|Proteomes:UP000265848};
RA   Zhang Y.-J.;
RT   "Pseudooceanicola sediminis CY03 in the family Rhodobacteracea.";
RL   Submitted (AUG-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}.
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:RII39172.1}.
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DR   EMBL; QWJJ01000006; RII39172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399J5F0; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000265848; 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}.
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;  52503 MW;  4B3AB6AE4BFE16FA CRC64;
     MQPVKEPGFR QSVDLMFNRA VALMDLPPGL EEKIRVCNAT YTVRFGVRLR GQIQTFTGYR
     SVHSEHMEPV KGGIRYALSV NQNEVEALAA LMTYKCALVE APFGGSKGGL CIDPRDWDDH
     ELEQITRRFA YELIKRDMIN PAQNVPAPDM GTGEREMAWI ADQYARMNTT DINSKACVTG
     KPLNAGGIAG RVEATGRGVQ YALQEFFREP EDKKKAGLSG TLDGKRVIVQ GLGNVGYHAA
     LFLSTEDGAR ITGIVERDGA LFNPEGLDVE AVREWINRHG GVTGYPEGQF VTDGASVMEE
     ECDILIPAAL EGVLNLENAE RIQAPLIIEA ANGPITAGAD EILRRKGCVI IPDLFANAGG
     VTVSYFEWVK NLSHIRFGRM QRRQEEARHQ LIVDELERLS ADSGIGWQLS PGFKDKYLRG
     AGELELVRSG LDDTMRTAYQ SMRAVWHARG DVEDLRTAAY LVAIDRVASS YRAKGL
//