MULTISPECIES: bifunctional 2-methylcitrate synthase/citrate

LOCUS       WP_003103050             375 aa            linear   BCT 25-FEB-2025
            synthase [Pseudomonas].
ACCESSION   WP_003103050
VERSION     WP_003103050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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..375
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..375
                     /gene="prpC"
     Protein         1..375
                     /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=41559
     Region          1..375
                     /region_name="PRK12351"
                     /note="methylcitrate synthase; Provisional"
                     /db_xref="CDD:183463"
     Site            order(10..12,15..19,81..82,85..86,94,98,102,105,150,
                     187..191,194..195,199,202..205,208,215..216,218..221,262,
                     353..363)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99861"
     Site            order(13,187,190,221..223,225,228,255..262,265,270,305,
                     307,310,312,333,337,353,356)
                     /site_type="active"
                     /db_xref="CDD:99861"
     Site            order(13,187,190,221..222,255..256,258..262,270,310,337)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99861"
     Site            order(187,190,222..223,261,270,312,333,337,356)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99861"
     Site            order(221..222,225,228,255..260,262,265,305,307,310,312,
                     353)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99861"
     Site            order(222,261,312)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99861"
ORIGIN      
        1 maeakvlsga glrgqvagqt alstvgqega gltyrgydvr dlaaaaifee vaylllygel
       61 pnkqqldayl kklqgqrdlp qalkevleri pkdahpmdvm rtgasvlgtl epelsfdqqr
      121 dvadrllaaf paimtywyrf thegqridcn sdeptigghf lallhgkkps elhvkvmnvs
      181 lilyaehefn astftarvca stlsdlyscv tgaigslrgp lhgganeaam elierfsspq
      241 eataellkml erkdkimgfg haiykdsdpr nevikgwskq ladevgdkvl favseaidkt
      301 mweqkklfpn adfyhasayh fmgiptklft pifvcsrtsg wtahvfeqra nnriirpsae
      361 ytgveqrafv pleqr