ID A0A1J6XAX7_9MICO Unreviewed; 356 AA.
AC A0A1J6XAX7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:OIU87294.1};
GN ORFNames=BFN01_09950 {ECO:0000313|EMBL:OIU87294.1};
OS Microbacterium sp. AR7-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1891970 {ECO:0000313|EMBL:OIU87294.1, ECO:0000313|Proteomes:UP000183831};
RN [1] {ECO:0000313|EMBL:OIU87294.1, ECO:0000313|Proteomes:UP000183831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR7-10 {ECO:0000313|EMBL:OIU87294.1,
RC ECO:0000313|Proteomes:UP000183831};
RA Pei D., Jiang J., Chen H., Li K., Yu W., Ma Y., Xu J.;
RT "The draft genome of Microbacterium sp. AR7-10 isolated from the wild
RT caught mosquito Anopheles.";
RL Submitted (SEP-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|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:OIU87294.1}.
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DR EMBL; MJIR01000061; OIU87294.1; -; Genomic_DNA.
DR RefSeq; WP_071643553.1; NZ_MJIR01000061.1.
DR AlphaFoldDB; A0A1J6XAX7; -.
DR STRING; 1891970.BFN01_09950; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000183831; 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; cd01075; NAD_bind_Leu_Phe_Val_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; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 146..354
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 184..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 356 AA; 36665 MW; 457CB949C75462A0 CRC64;
MSHTLPLPDF THERVEVTTG RRSGLFIAVA LHSSVLGSAL GGARLWTYPH WSDALGDALR
LSAAMTLKNA AAGLDAGGGK SVIGLAPGET LDAERRRDAF LDLGDAVELM GGLYRTAEDV
GSTTDDMLTV SERTQHVVGL PSAVGGSGEP AGPTSLGVYA SLQAVLERVT GSADAAGRRI
TISGLGQVGG RLAVRLAEQG AQLTVTDINP ARRAFADEIG ATWVEPGAEH LVAGDVFVPA
GIGGVLTDEI IDALDVKAVC GPANNPLADR SGADRLAQRG VLYAPDFVVN AGGVIYLDLE
AKRIGSSEEI MHRVAGIGDT VRRILDDADA RGVTPLLAAE ELAASRLRAG TAVGAR
//