ID   A0A2T7FWM7_9RHOB        Unreviewed;       480 AA.
AC   A0A2T7FWM7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=DC363_08525 {ECO:0000313|EMBL:PVA06572.1};
OS   Thalassorhabdomicrobium marinisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thalassorhabdomicrobium.
OX   NCBI_TaxID=2170577 {ECO:0000313|EMBL:PVA06572.1, ECO:0000313|Proteomes:UP000244817};
RN   [1] {ECO:0000313|EMBL:PVA06572.1, ECO:0000313|Proteomes:UP000244817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH-SD16 {ECO:0000313|EMBL:PVA06572.1,
RC   ECO:0000313|Proteomes:UP000244817};
RA   Ji X.;
RT   "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT   Bohai Sea.";
RL   Submitted (APR-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:PVA06572.1}.
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DR   EMBL; QCYG01000005; PVA06572.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7FWM7; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000244817; 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:UP000244817}.
FT   DOMAIN          192..479
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        111
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         238
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            153
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   480 AA;  53197 MW;  60550C2814866F85 CRC64;
     MSTTPAHLQE PSFRESVDIM FNRAVALMDL SPGLEEKIRV CNATYTVRFG VRLRGKIETF
     TGYRSVHSEH MEPVKGGIRY SMNVNQNEVE ALAALMTYKC ALVETPFGGS KGGLCIDPRE
     WDEEELERIT RRFAYELAKR DLIHPSQNVP APDMGTGERE MAWIADQYRR MNTTDINAAA
     CVTGKPAHAG GIQGRVEATG RGVQYALKEF FRHPEDVQIA GLSGTLDGKR VIVQGLGNVG
     FHAAKFLREE DGCKITGIIE HDGALVDENG LDVPAVREWI GKTGGVKGYP DGKYVENGAS
     VLEHDCDILI PAAMEGVINK GNAPRIQAPL IIEAANGPVT AGADEILREK GTVMIPDMYA
     NAGGVTVSYF EWVKNLSHIR FGRMQRRQEE ARHELIVGEL ERLSEHMGDQ WSMTPNFKQK
     YLRGAGELEL VRSGLDDTMR TAYQAMREVW HSREDVTDLR TAAYLVSIGR VATSYRAKGL
//