ID A0A2U2ZJ67_9ACTN Unreviewed; 362 AA.
AC A0A2U2ZJ67;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Valine dehydrogenase {ECO:0000256|ARBA:ARBA00017332};
DE EC=1.4.1.23 {ECO:0000256|ARBA:ARBA00012136};
GN ORFNames=DIZ27_01750 {ECO:0000313|EMBL:PWI12327.1};
OS Streptomyces sp. NWU339.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI12327.1, ECO:0000313|Proteomes:UP000245372};
RN [1] {ECO:0000313|EMBL:PWI12327.1, ECO:0000313|Proteomes:UP000245372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWU339 {ECO:0000313|EMBL:PWI12327.1,
RC ECO:0000313|Proteomes:UP000245372};
RA Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT South African rhizosphere soils.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-valine + NAD(+) = 3-methyl-2-oxobutanoate + H(+) +
CC NADH + NH4(+); Xref=Rhea:RHEA:30763, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57762, ChEBI:CHEBI:57945; EC=1.4.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001280};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000256|ARBA:ARBA00005109}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PWI12327.1}.
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DR EMBL; QFRK01000001; PWI12327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZJ67; -.
DR OrthoDB; 9803297at2; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000245372; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0043837; F:valine dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
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; IPR006115; 6PGDH_NADP-bd.
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 Pfam; PF03446; NAD_binding_2; 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 Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245372}.
FT DOMAIN 152..362
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 362 AA; 38171 MW; 94212700F8B656D8 CRC64;
MTDVSDGVLH TLFRSDQGGH EQVVLCQDRA SGLKAVIALH STALGPALGG TRFYPYATEE
QAVADALNLA RGMSYKNAMA GLDHGGGKAV IIGDPETVKS EELLLAYGRF VASLGGRYVT
ACDVGTYVAD MDVVARECRW TTGRSPENGG AGDSSVLTSF GVYQGMRAAA QHLWGDPSLR
DRKVGVAGVG KVGHHLVEHL LKEGAEVLVT DVREDAVRRV LDRHPRGVTA VADTEALIRA
EGLDVYAPCA LGGALNDDSV PVLTAKVVCG AANNQLAHPG VEKDLADRGI LYAPDYVVNA
GGVIQVADEL HGFDFDRCRA KAAKIFDTTL AIFTRAKSDG IPPAAAADRI AEQRMAEARA
AR
//
