MULTISPECIES: dTDP-glucose 4,6-dehydratase [Escherichia].

LOCUS       WP_000699460             361 aa            linear   BCT 17-JUN-2024
ACCESSION   WP_000699460
VERSION     WP_000699460.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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..361
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..361
                     /gene="rfbB"
     Protein         1..361
                     /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=40427
     Region          1..352
                     /region_name="PRK10084"
                     /note="dTDP-glucose 4,6 dehydratase; Provisional"
                     /db_xref="CDD:236649"
     Site            order(7,9..12,32..35,37..38,57..59,80..82,84,99,131..133,
                     167,171,194..197)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187557"
     Site            order(84..86,133..135,167,194..196,205..207,210..211,
                     222..224,229,231,266,297,300,304)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187557"
     Site            order(88,90,93..94,97,101..102,105,109,112,139,158,
                     160..161,163..166,169,172..173,176..177,180..181,183..185,
                     301)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187557"
     Site            order(100,133,167,171)
                     /site_type="active"
                     /db_xref="CDD:187557"
ORIGIN      
        1 mkilvtggag figsavvrhi inntqdsvvn vdkltyagnr esladvsdse ryvfehadic
       61 dapamarifa qhqpdavmhl aaeshvdrsi tgpaafietn ivgtyvllea arnywsalds
      121 dkknsfrfhh istdevygdl phpdevnnte elplftetta yapsspysas kassdhlvra
      181 wkrtyglpti vtncsnnygp yhfpeklipl vilnalegka lpiygkgdqi rdwlyvedha
      241 ralytvvteg kagetynigg hnekknidvv lticdlldei vpkeksyreq ityvadrpgh
      301 drryaidaek igralgwkpq etfesgirkt vewylsntkw vdnvksgayq swieqnyegr
      361 q