ID   A0A1Z9RKR0_9RICK        Unreviewed;       466 AA.
AC   A0A1Z9RKR0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=CBE11_00380 {ECO:0000313|EMBL:OUX17079.1};
OS   Rickettsiales bacterium TMED251.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX   NCBI_TaxID=1986870 {ECO:0000313|EMBL:OUX17079.1, ECO:0000313|Proteomes:UP000195709};
RN   [1] {ECO:0000313|EMBL:OUX17079.1, ECO:0000313|Proteomes:UP000195709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED251 {ECO:0000313|EMBL:OUX17079.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-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:OUX17079.1}.
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DR   EMBL; NHKW01000003; OUX17079.1; -; Genomic_DNA.
DR   Proteomes; UP000195709; 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          186..465
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         193
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            147
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   466 AA;  51881 MW;  6A683D82B4B76E99 CRC64;
     MLSGKEFLHS VEQVFDNAAK ALKLPESLSN QIKSANATYK VNFGVRIKNK ISTFTGFRCV
     HSDHLEPVKG GIRYAINSDQ NEVEALAALM TYKCALVDIP FGGSKGALIL DPKIYKIQDX
     ERITRRFAQE LIKRDLINPS QNVPAPDMGT GEREMAWIAD EYRKLNPTDI NSSACVTGKP
     INYNGIRGRS EATGRGVQYA IREFFRHKKD VKIAKFQGDI EGKKIIIQGL GNVGYHAAKF
     LSKDDGAIIT GVIEXDGGVI NDKGIDIENL SKFIKKNGGV KGYKGFVKNG SDLLKKECDI
     LIPAALEGVI NKTNVREIKA NLIVEAANGP ITYEADKFLN KKKVIIPDLY ANAGGVTVSY
     FEWVKNLARI RFGRLQKREE ENKIIKLIEN METLTGKKTL AIERSKILKG ADELDLVRSG
     LDDTMREAYQ TMSYKWHSNK HVKDLRTSAM TIALQKIANS YEILGI
//