MULTISPECIES: bifunctional 2-methylcitrate synthase/citrate

LOCUS       WP_001285914             389 aa            linear   BCT 25-FEB-2025
            synthase [Enterobacteriaceae].
ACCESSION   WP_001285914
VERSION     WP_001285914.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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 :: NF009006.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK12351
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..389
                     /gene="prpC"
     Protein         1..389
                     /product="bifunctional 2-methylcitrate synthase/citrate
                     synthase"
                     /EC_number="2.3.3.16"
                     /EC_number="2.3.3.5"
                     /GO_function="GO:0004108 - citrate (Si)-synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050440 - 2-methylcitrate synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0019679 - propionate metabolic process,
                     methylcitrate cycle [Evidence IEA]"
                     /calculated_mol_wt=42976
     Region          15..388
                     /region_name="PRK12351"
                     /note="methylcitrate synthase; Provisional"
                     /db_xref="CDD:183463"
     Site            order(20..22,25..29,91..92,95..96,104,108,112,115,163,
                     200..204,207..208,212,215..218,221,228..229,231..234,275,
                     366..376)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99870"
     Site            order(23,200,203,234..236,238,241,268..275,278,283,318,
                     320,323,325,346,350,366,369)
                     /site_type="active"
                     /db_xref="CDD:99870"
     Site            order(23,200,203,234..235,268..269,271..275,283,323,350)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99870"
     Site            order(200,203,235..236,274,283,325,346,350,369)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99870"
     Site            order(234..235,238,241,268..273,275,278,318,320,323,325,
                     366)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99870"
     Site            order(235,274,325)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99870"
ORIGIN      
        1 msdttilqns thvikpkksv alsgvpagnt alctvgksgn dlhyrgydil dlaehcefee
       61 vahllihgkl ptrdelaayk tklkalrglp anvrtvleal paashpmdvm rtgvsalgct
      121 lpekeghtvs gardiadkll aslssillyw yhyshngeri qpetdddsig ghflhllhge
      181 kpsqswekam hislvlyaeh efnastftsr viagtgsdmy saiigaigal rgpkhggane
      241 vsleiqqrye tpdeaeadir krveskevvi gfghpvytia dprhqvikrv akqlsqeggs
      301 lkmyniadrl etvmweskkm fpnldwfsav synmmgvpte mftplfviar vtgwaahiie
      361 qrqdnkiirp sanyvgpedr qfvaldkrq