bifunctional 2-methylcitrate dehydratase/aconitate hydratase

LOCUS       WP_017015987             483 aa            linear   BCT 10-AUG-2020
            [Enterovibrio norvegicus].
ACCESSION   WP_017015987
VERSION     WP_017015987.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio norvegicus
  ORGANISM  Enterovibrio norvegicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Enterovibrio.
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="Enterovibrio norvegicus"
                     /db_xref="taxon:188144"
     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=53965
     Region          2..482
                     /region_name="prpD"
                     /note="bifunctional 2-methylcitrate dehydratase/aconitate
                     hydratase; PRK09425"
                     /db_xref="CDD:181845"
ORIGIN      
        1 msqnvdinqr pepdallqti adyvceteid saeayntarn clmdtlgcgl lalrfpectk
       61 hmgplvpgtt vrhgarvpgt sheldpitaa fnigcmirwl dfndtwlaae wghpsdnlgg
      121 ilatadylsr vaiaegnapl tmrdvltami kaheiqgvma lensynrvgl dhvllvrvas
      181 tavvtrmlgg nrdqvidals qawvdgcslr tyrhapnags rkswaagdat sravrlamit
      241 mkgemglpsv ltaekwgfyd vlfkgeafrv nqpfnsyvme nvlfkisfpa efhaqtavec
      301 avtlhpqikd rldeidriev tthesairii skvgdlanpa drdhclqyml avplihgdli
      361 aehyeddfhr ndpridalrd kmviqedtry seeyldpekr sianavqvff tdgssterve
      421 veypighrrr reegipvlea kfkrnlqtrf psaqtekiya lccdqdtlmt tpvttfmemf
      481 sin