MULTISPECIES: O-antigen biosynthesis phosphomannomutase RfbK

LOCUS       WP_001103643             477 aa            linear   BCT 06-APR-2020
            [Salmonella].
ACCESSION   WP_001103643
VERSION     WP_001103643.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Jiang,X.M., Neal,B., Santiago,F., Lee,S.J., Romana,L.K. and
            Reeves,P.R.
  TITLE     Structure and sequence of the rfb (O antigen) gene cluster of
            Salmonella serovar typhimurium (strain LT2)
  JOURNAL   Mol. Microbiol. 5 (3), 695-713 (1991)
   PUBMED   1710759
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  :: BlastRule
            Evidence Accession :: NBR011762
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..477
                     /gene="rfbK"
     Protein         1..477
                     /product="O-antigen biosynthesis phosphomannomutase RfbK"
                     /calculated_mol_wt=51955
     Region          18..468
                     /region_name="ManB"
                     /note="ManB is a bacterial phosphomannomutase (PMM) that
                     catalyzes the conversion of mannose 6-phosphate to
                     mannose-1-phosphate in the second of three steps in the
                     GDP-mannose pathway, in which GDP-D-mannose is synthesized
                     from fructose-6-phosphate. In...; cd03088"
                     /db_xref="CDD:100090"
     Site            order(19,21,24,111..113,121,245,247,249..250,284,303..305,
                     326,328,330,440,442..444,449)
                     /site_type="active"
                     /db_xref="CDD:100090"
     Site            order(21,111,250,284,303,305,326,328,330,440,442..444,449)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100090"
     Site            order(111,245,247,249)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100090"
ORIGIN      
        1 mnvvnnsrdv iyssgivfgt sgarglvkdf tpqvcaaftv sfvavmqehf sfdtvalaid
       61 nrpssygmaq acaaaladkg vncifygvvp tpalafqsms dnmpaimvtg shipferngl
      121 kfyrpdgeit khdeaailsv edtcshlelk elivsemaav nyisrytslf stpflknkri
      181 giyehssagr dlykplfial gaevvslgrs dnfvpidtea vskedrekar swakefdlda
      241 ifstdgdgdr pliadeagew lrgdilgllc slaldaeava ipvscnsiis sgrffkhvkl
      301 tkigspyvie afnelsrsys rivgfeangg fllgsdicin eqnlhalptr davlpaimll
      361 yksrntsisa lvnelptryt hsdrlqgitt dksqslismg renlsnllsy iglenegais
      421 tdmtdgmrit lrdgcivhlr asgnapelrc yaeanllnra qdlvnttlan ikkrcll