triose-phosphate isomerase [Listeria monocytogenes].

LOCUS       WP_010989434             254 aa            linear   BCT 23-DEC-2024
ACCESSION   WP_010989434
VERSION     WP_010989434.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Nagano,N., Orengo,C.A. and Thornton,J.M.
  TITLE     One fold with many functions: the evolutionary relationships
            between TIM barrel families based on their sequences, structures
            and functions
  JOURNAL   J Mol Biol 321 (5), 741-765 (2002)
   PUBMED   12206759
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wierenga,R.K.
  TITLE     The TIM-barrel fold: a versatile framework for efficient enzymes
  JOURNAL   FEBS Lett 492 (3), 193-198 (2001)
   PUBMED   11257493
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10085182
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..254
                     /product="triose-phosphate isomerase"
                     /EC_number="5.3.1.1"
                     /GO_function="GO:0004807 - triose-phosphate isomerase
                     activity [Evidence IEA]"
                     /GO_function="GO:0031625 - ubiquitin protein ligase
                     binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27787
     Region          4..247
                     /region_name="TIM"
                     /note="Triosephosphate isomerase (TIM) is a glycolytic
                     enzyme that catalyzes the interconversion of
                     dihydroxyacetone phosphate and
                     D-glyceraldehyde-3-phosphate. The reaction is very
                     efficient and requires neither cofactors nor metal ions.
                     TIM, usually...; cd00311"
                     /db_xref="CDD:238190"
     Site            order(9,11,96,168,174,212,231,233..234)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(9,12,45..47,49,52,65,83,86..87,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(11,96,168)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
ORIGIN      
        1 mrkplvginm knyintraqt sewleatipl lgnfsdvdtf ifpsmgtlet tanllagtsf
       61 gfgpqnmape ksgpltgefs vesiidlsan yveighaerk nlfhektsei akkiqlalde
      121 kitpvvcvge girandtnel knalkkqiea lfdtiqvtqf knvvlayepe waigkansad
      181 tdyiesahqa lreiirelgg detlvriiyg gsvskenaae ivrqknvdgl fvgrfghkpq
      241 nfadivsivs ktkg