MULTISPECIES: bifunctional 2-methylcitrate dehydratase/aconitate

LOCUS       WP_000107071             483 aa            linear   BCT 10-SEP-2020
            hydratase [Salmonella].
ACCESSION   WP_000107071
VERSION     WP_000107071.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Brock,M., Maerker,C., Schutz,A., Volker,U. and Buckel,W.
  TITLE     Oxidation of propionate to pyruvate in Escherichia coli.
            Involvement of methylcitrate dehydratase and aconitase
  JOURNAL   Eur. J. Biochem. 269 (24), 6184-6194 (2002)
   PUBMED   12473114
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Gulick,A.M., Horswill,A.R., Thoden,J.B., Escalante-Semerena,J.C.
            and Rayment,I.
  TITLE     Pentaerythritol propoxylate: a new crystallization agent and
            cryoprotectant induces crystal growth of 2-methylcitrate
            dehydratase
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 58 (Pt 2), 306-309 (2002)
   PUBMED   11807258
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Horswill,A.R. and Escalante-Semerena,J.C.
  TITLE     In vitro conversion of propionate to pyruvate by Salmonella
            enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase
            Enzymes catalyze the conversion of 2-methylcitrate to
            2-methylisocitrate
  JOURNAL   Biochemistry 40 (15), 4703-4713 (2001)
   PUBMED   11294638
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 :: NF006943.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09425
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..483
                     /product="bifunctional 2-methylcitrate
                     dehydratase/aconitate hydratase"
                     /EC_number="4.2.1.3"
                     /EC_number="4.2.1.79"
                     /GO_function="GO:0047547 - 2-methylcitrate dehydratase
                     activity [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0019679 - propionate metabolic process,
                     methylcitrate cycle [Evidence IEA]"
                     /calculated_mol_wt=53656
     Region          1..483
                     /region_name="prpD"
                     /note="bifunctional 2-methylcitrate dehydratase/aconitate
                     hydratase; PRK09425"
                     /db_xref="CDD:181845"
ORIGIN      
        1 mstqelnirp dfdreivdiv dyvmnyeits kvaydtahyc lldtlgcgle aleypackkl
       61 lgpivpgtvv pngarvpgtq fqldpvqaaf nigamirwld fndtwlaaew ghpsdnlggi
      121 latadwlsrn avaagkaplt mkqvlsgmik aheiqgcial enafnrvgld hvllvkvast
      181 avvaemlglt rdeilnavsl awvdgqslrt yrhapntgtr kswaagdats ravrlalmak
      241 tgemgypsal taktwgfydv sfkgetfrfq rpygsyvmen vlfkisfpae fhsqtaveaa
      301 mtlyeqmqaa gktaadiekv tirtheaclr iidkkgplnn padrdhciqy mvavpllfgr
      361 ltaadyedev aqdkridalr ekivcyedpa ftadyhdpek raignaitve ftdgsrfgev
      421 vveypighar rradgipkli ekfkinlarq fptrqqqril dvsldrarle qmpvneyldl
      481 yvi