ID M2Z7R4_9NOCA Unreviewed; 357 AA.
AC M2Z7R4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Valine dehydrogenase (ValDH) {ECO:0000313|EMBL:EME63312.1};
GN ORFNames=G352_15093 {ECO:0000313|EMBL:EME63312.1};
OS Rhodococcus ruber BKS 20-38.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1278076 {ECO:0000313|EMBL:EME63312.1, ECO:0000313|Proteomes:UP000011731};
RN [1] {ECO:0000313|EMBL:EME63312.1, ECO:0000313|Proteomes:UP000011731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 20-38 {ECO:0000313|EMBL:EME63312.1,
RC ECO:0000313|Proteomes:UP000011731};
RX PubMed=23558535;
RA Bala M., Kumar S., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Rhodococcus ruber Strain BKS 20-38.";
RL Genome Announc. 1:E0013913-E0013913(2013).
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:EME63312.1}.
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DR EMBL; AOEX01000044; EME63312.1; -; Genomic_DNA.
DR RefSeq; WP_003937104.1; NZ_AOEX01000044.1.
DR AlphaFoldDB; M2Z7R4; -.
DR PATRIC; fig|1278076.4.peg.3125; -.
DR Proteomes; UP000011731; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {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 157..357
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 93
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 193..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 357 AA; 36654 MW; 1BBEB43A1DEBBF61 CRC64;
MTASLLDHAP TGVFDRSRRL SDRPHEQVVF CQDAATGLRA IVAIHSTALG PALGGTRFYP
YADEATALED VLRLSWGMTY KAAVAGVNLG GGKAVILGDP ATDKSDALLA AYGRFVESLG
GRYVTAADVG TAAGDLDVVG RHTRYAVGRT AAAGGSGDSS PLTALGVFRA MRAGAEHVWG
TASLDGRTVG VEGLGKVGYE LVRLLVADGA DVVVTDVNPA ALARVAADFP VRIASNVVDA
PVDVYAPCAL GGTLTTSAGS TLGARLVCGA ANNQLARPEV EDLLRDRGIT WVPDYVANAG
GLIQVAGEVD GSDPSVVRSR VNAIFDRTAE IFAMSRDLGI GPGAAANRLA EQRIDAA
//
