ID   Q0FF08_9RHOB            Unreviewed;       471 AA.
AC   Q0FF08;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=OM2255_06615 {ECO:0000313|EMBL:EAU53181.1};
OS   Rhodobacterales bacterium HTCC2255.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU53181.1, ECO:0000313|Proteomes:UP000009381};
RN   [1] {ECO:0000313|EMBL:EAU53181.1, ECO:0000313|Proteomes:UP000009381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU53181.1,
RC   ECO:0000313|Proteomes:UP000009381};
RA   Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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:EAU53181.1}.
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DR   EMBL; AATR01000001; EAU53181.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0FF08; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_1_0_5; -.
DR   OrthoDB; 9803297at2; -.
DR   BioCyc; RBAC367336:G1GNW-768-MONOMER; -.
DR   Proteomes; UP000009381; 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:UP000009381}.
FT   DOMAIN          188..470
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   471 AA;  51731 MW;  B798C1EA129DF7BB CRC64;
     MTSRTEPTFR ESVNMMFDKA ISLIDISPGL AQKIKVCNST YTVRFGVKLR GDIHTFTGYR
     SVHSEHKEPV KGGIRFATSV NQDEVEALAA LMTYKCALVE APFGGSKGGL HIDPTQWEPD
     EIEKITRRFA YELIKRDLIH PSQNVPAPDM GTGEREMAWI ADQFRRMNTS EINADACVTG
     KPLNKGGIIG RVEATGRGVQ YALQEFFRHK DDVKTSGLSG SLAGKRIIVQ GLGNVGYHAA
     HFLSTEDGCK ITAVIERDGA VINDDGININ QLQTHLIENK GVKGFSGANY VSNGSEILEK
     DCDILIPAAM EGVINLSNAQ RIKANVIIEA ANGPVTAGAD EILTAAGTII IPDMYANAGG
     VTVSYFEWVK NLSHIRFGRM QRRQQASSNH ILVEEMERLI GKPVSEDFKN KFFKGAGELE
     LVRSGLEDTM CTAYQQMHDT WRSNENIDSL RTAAYVLALT KVADSYRALG L
//