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Database: UniProt
Entry: A4X194_SALTO
LinkDB: A4X194_SALTO
Original site: A4X194_SALTO 
ID   A4X194_SALTO            Unreviewed;       360 AA.
AC   A4X194;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   SubName: Full=Valine dehydrogenase (NAD) {ECO:0000313|EMBL:ABP52644.1};
DE            EC=1.4.1.- {ECO:0000313|EMBL:ABP52644.1};
GN   OrderedLocusNames=Strop_0159 {ECO:0000313|EMBL:ABP52644.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS   105044 / CNB-440).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP52644.1, ECO:0000313|Proteomes:UP000000235};
RN   [1] {ECO:0000313|Proteomes:UP000000235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC   {ECO:0000313|Proteomes:UP000000235};
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; CP000667; ABP52644.1; -; Genomic_DNA.
DR   RefSeq; WP_011904081.1; NC_009380.1.
DR   AlphaFoldDB; A4X194; -.
DR   STRING; 369723.Strop_0159; -.
DR   KEGG; stp:Strop_0159; -.
DR   PATRIC; fig|369723.5.peg.163; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_0_0_11; -.
DR   OMA; TYVADMD; -.
DR   Proteomes; UP000000235; Chromosome.
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; 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|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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000235}.
FT   DOMAIN          147..356
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        83
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT   BINDING         183..188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ   SEQUENCE   360 AA;  37883 MW;  BE13BCC3E1C468A0 CRC64;
     MGVFATTDAP ASVGHEQVVF CQDKQSGLRA IIGIYSTALG PALGGTRFYP YASEEAALAD
     VLDLSRGMAY KNALAGLDLG GGKAVIWGDP EQLKSETLLR AYGRFVATLG GRYYTACDVG
     TYVADMDVIA RETRFVTGRS REHGGAGDSS ILTAWGVFQG MRAAAEHAWG TSTLRGRRVG
     VAGLGKVGKH LVGHLLDDGA EVVATDVNPR ALAWARTTHP QVTLLDDASA LAASDIDVYA
     PCALGGTLND HTVPALRATV VAGAANNQLA HPGIEKLLAD RGILYAPDYV VNAGGVIQVA
     DEIEGFNFDR AKLRATKIYD TTREILGLAD AEGVPPAVAA DRLAERRMAE VGRLRTVLLP
//
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