fructose-6-phosphate aldolase [Escherichia coli].

LOCUS       WP_000424823             220 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_000424823
VERSION     WP_000424823.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 220)
  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..220
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..220
                     /gene="fsa"
     Protein         1..220
                     /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=23375
     Region          1..220
                     /region_name="TIM-like beta/alpha barrel domains"
                     /note="A large family of domains similar to triose
                     phosphate isomerase (TIM) which, in general, share an
                     eight beta/alpha closed barrel structure; cl21457"
                     /db_xref="CDD:473867"
     Site            order(6,27..28,85,131,165)
                     /site_type="active"
                     /db_xref="CDD:188643"
     Site            order(17,20,29..30,33,36,40,59,65,71,91,93..94,97,116,131,
                     133,136,138,155..156,169,171,177..178,181,197,199..200,
                     203,207..208,210..211)
                     /site_type="active"
                     /note="intersubunit interactions [active]"
                     /db_xref="CDD:188643"
     Site            85
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188643"
ORIGIN      
        1 melyldtanv aeverlahif piagvttnps iiaaskesiw evlprlqkai gdegilfaqt
       61 msrdaqgmve eakrlrdaip givvkipvts eglaaikilk kegittlgta vysaaqglla
      121 alagakyvap yvnrvdaqgg dgirtvqelq allemhapes mvlaasfktp rqaldcllag
      181 cesitlpldv aqqmlntpav esaiekfehd wnaafgtthl