MULTISPECIES: dTDP-4-dehydrorhamnose reductase [Pseudomonas].

LOCUS       WP_003113045             294 aa            linear   BCT 27-JUL-2024
ACCESSION   WP_003113045
VERSION     WP_003113045.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Giraud,M.F. and Naismith,J.H.
  TITLE     The rhamnose pathway
  JOURNAL   Curr Opin Struct Biol 10 (6), 687-696 (2000)
   PUBMED   11114506
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12051926
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..294
                     /product="dTDP-4-dehydrorhamnose reductase"
                     /EC_number="1.1.1.133"
                     /GO_function="GO:0008831 - dTDP-4-dehydrorhamnose
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32809
     Region          5..291
                     /region_name="RmlD_sub_bind"
                     /note="RmlD substrate binding domain; pfam04321"
                     /db_xref="CDD:427865"
ORIGIN      
        1 mrmrlmllgg gnalgqalir lgaeedigfl aprppeqgwd aaslttllde trpdavinla
       61 fyhdwfqaeq veaerlgaqe raverlaelc qhyeillvqp ssyrvfdgar ataysekdet
      121 lplglrgqal wrmeqsvraa cprhvlirfg wlldespngl lgrflsraeq pqplfladdr
      181 rgnptpvdda arvvlsvlkq ldcqaplwgt yhyggleatt tlalgqviln eartyrsnli
      241 qepsaeahaa rpdaldepqh avmvckkilh tfgikprawr aglpalldry yrhv