fructose-6-phosphate aldolase [Shigella flexneri].

LOCUS       WP_001249351             244 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_001249351
VERSION     WP_001249351.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schurmann,M. and Sprenger,G.A.
  TITLE     Fructose-6-phosphate aldolase is a novel class I aldolase from
            Escherichia coli and is related to a novel group of bacterial
            transaldolases
  JOURNAL   J Biol Chem 276 (14), 11055-11061 (2001)
   PUBMED   11120740
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 :: TIGR00875.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..244
                     /gene="fsa"
     Protein         1..244
                     /product="fructose-6-phosphate aldolase"
                     /GO_function="GO:0016832 - aldehyde-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25948
     Region          25..244
                     /region_name="PRK12653"
                     /note="fructose-6-phosphate aldolase; Reviewed"
                     /db_xref="CDD:183653"
     Site            order(30,51..52,109,155,189)
                     /site_type="active"
                     /db_xref="CDD:188643"
     Site            order(41,44,53..54,57,59,63,83,89,95,115,117..118,121,140,
                     155,157,160,162,179..180,193,195,201..202,205,221,
                     223..224,227,231..232,234..235)
                     /site_type="active"
                     /note="intersubunit interactions [active]"
                     /db_xref="CDD:188643"
     Site            109
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188643"
ORIGIN      
        1 mrqlfrefsr dslhsdkkyi lrmvmelyld tsdvvavkal srifplagvt tnpsiiaagk
       61 kpldvvlpql heamggqgrl faqvmattae gmvndalklr siiadivvkv pvtaeglaai
      121 kmlkaegipt lgtavygaaq gllsalagae yvapyvnrid aqggsgiqtv tdlhqllkmh
      181 apqakvlaas fktprqaldc llagcesitl pldvaqqmis ypaveaavtk feqdwqgafg
      241 rtsi