dTDP-glucose 4,6-dehydratase [Enterovibrio norvegicus].

LOCUS       WP_017007827             353 aa            linear   BCT 17-JUN-2024
ACCESSION   WP_017007827
VERSION     WP_017007827.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio norvegicus
  ORGANISM  Enterovibrio norvegicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Enterovibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01181.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Enterovibrio norvegicus"
                     /db_xref="taxon:188144"
     gene            1..353
                     /gene="rfbB"
     Protein         1..353
                     /product="dTDP-glucose 4,6-dehydratase"
                     /EC_number="4.2.1.46"
                     /GO_function="GO:0008460 - dTDP-glucose 4,6-dehydratase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009225 - nucleotide-sugar metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=39496
     Region          1..347
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..12,32..35,37..38,57..59,80..82,84,99,131..133,
                     159,163,186..189)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187557"
     Site            order(84..86,133..135,159,186..188,197..199,202..203,
                     214..216,221,223,258,293,296,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187557"
     Site            order(88,90,93..94,97,101..102,105,109,112,139,150,
                     152..153,155..158,161,164..165,168..169,172..173,175..177,
                     297)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187557"
     Site            order(100,133,159,163)
                     /site_type="active"
                     /db_xref="CDD:187557"
ORIGIN      
        1 mkilvtggag figsavvrhi iqntqdsvin vdkltyagnl eslsdveknd ryafveadic
       61 nrgamddifa tyqpdavmhl aaeshvdrsi dgpaafietn ivgtytlles araywnqlde
      121 drkatfkfhh istdevygdl egtddlfset tsyapsspys askassdhlv rawqrtygfp
      181 tlvtncsnny gpfhfpekli plmilnaleg kalpvygdgm qirdwlfved haralykvat
      241 egevgetyni gghnekanid vvkticalle elvpnkpsgv kqysdlityv kdrpghdvry
      301 aidaskieke lgwkpeetfe sgirktvewy lnnqewwsrv ldgsytrqrl gsn