alpha amylase C-terminal domain-containing protein [Escherichia

LOCUS       WP_001304065             335 aa            linear   BCT 01-MAR-2025
            coli].
ACCESSION   WP_001304065
VERSION     WP_001304065.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Strobl,S., Maskos,K., Betz,M., Wiegand,G., Huber,R.,
            Gomis-Ruth,F.X. and Glockshuber,R.
  TITLE     Crystal structure of yellow meal worm alpha-amylase at 1.64 A
            resolution
  JOURNAL   J Mol Biol 278 (3), 617-628 (1998)
   PUBMED   9600843
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Larson,S.B., Greenwood,A., Cascio,D., Day,J. and McPherson,A.
  TITLE     Refined molecular structure of pig pancreatic alpha-amylase at 2.1
            A resolution
  JOURNAL   J Mol Biol 235 (5), 1560-1584 (1994)
   PUBMED   8107092
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 :: NF014822.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF02806.24
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..335
                     /product="alpha amylase C-terminal domain-containing
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043169 - cation binding [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37940
     Region          <1..225
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(19,21,66,135..136)
                     /site_type="active"
                     /db_xref="CDD:200454"
     Site            order(21,66,136)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200454"
     Region          236..323
                     /region_name="Alpha-amylase_C"
                     /note="Alpha amylase, C-terminal all-beta domain;
                     pfam02806"
                     /db_xref="CDD:426991"
ORIGIN      
        1 mlqnqyvrem rkygvrglry daakhskheq iersitpplk nynerlhntn lfnpkyheka
       61 vmnymeylvt cqldeeqmss llyerddlsa idfsllmkti kafsfggdlq tlaskpssti
      121 ssipskrril ininhdfpnn gnlfndflfn hqqdeqlama ymaalpfsrp lvywdgqvlk
      181 stteiknydg strvggeawl nkgcstyqql ynefhalyid kagiwsafeg vfatknvlaf
      241 srgdsvninh sphdglviin kgneevegaw pnklqpgkyk nmgsnsvnii inntrkiipp
      301 gkafmlrggt lninipgrsa lllgktgepl nylyl