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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//