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Database: UniProt
Entry: A0A1M5N2X4_9RHOB
LinkDB: A0A1M5N2X4_9RHOB
Original site: A0A1M5N2X4_9RHOB 
ID   A0A1M5N2X4_9RHOB        Unreviewed;       479 AA.
AC   A0A1M5N2X4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=SAMN05444003_1160 {ECO:0000313|EMBL:SHG83910.1};
OS   Cognatiyoonia sediminum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cognatiyoonia.
OX   NCBI_TaxID=1508389 {ECO:0000313|EMBL:SHG83910.1, ECO:0000313|Proteomes:UP000184074};
RN   [1] {ECO:0000313|EMBL:SHG83910.1, ECO:0000313|Proteomes:UP000184074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28715 {ECO:0000313|EMBL:SHG83910.1,
RC   ECO:0000313|Proteomes:UP000184074};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQXB01000001; SHG83910.1; -; Genomic_DNA.
DR   RefSeq; WP_072899881.1; NZ_FQXB01000001.1.
DR   AlphaFoldDB; A0A1M5N2X4; -.
DR   STRING; 1508389.SAMN05444003_1160; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000184074; 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:UP000184074}.
FT   DOMAIN          191..478
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            152
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   479 AA;  52681 MW;  644DB88008B0518D CRC64;
     MASSSSPKEP SFRESVDIMF NRAVALMGLP PGLEEKIRVC NATYTVRFGV RLRGDIHTFV
     GYRSVHSEHM EPVKGGIRYA GNVDQDEVEA LAALMTYKCA LVEAPFGGSK GGLCIDPREW
     DEHELEMITR RFAYELAKRD LIHPSQNVPA PDMGTGEREM AWIADQYRRM NTTDINSAAC
     VTGKPPNAGG IAGRVEATGR GVQYALQEFF RHPEDIAAAG LKGTLKDKRI IVQGLGNVGF
     HAAKFLSEED GAKITGIIER DGALRDDTGL DVEAVRAWIA ENGGVKGYDE ALYLEEGSAL
     LEEECDILIP AALEGVINLS NADRVKAPLI IEAANGPVTA GADEILRDKG CVIIPDMYAN
     AGGVTVSYFE WVKNLSHIRF GRMQRRAEES RHQLVVDELE RLSSDTGIGW ELSPDFKEKY
     LRGAGELELV RSGLDDTMRK AYQDMRKVWH SRDDVTDLRT AAYLVSIGKV ADSYKAKGL
//
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