sugar phosphorylase [Listeria monocytogenes].

LOCUS       WP_010990053             560 aa            linear   BCT 24-JUL-2024
ACCESSION   WP_010990053
VERSION     WP_010990053.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 560)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
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 10183418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..560
                     /product="sugar phosphorylase"
                     /EC_number="2.4.1.-"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63802
     Region          47..502
                     /region_name="AmyAc_Sucrose_phosphorylase-like_1"
                     /note="Alpha amylase catalytic domain found in sucrose
                     phosphorylase-like proteins (also called sucrose
                     glucosyltransferase, disaccharide glucosyltransferase, and
                     sucrose-phosphate alpha-D glucosyltransferase); cd11356"
                     /db_xref="CDD:200493"
     Site            order(98,101,136,192,196,226,228..229,232,270,272,
                     336..337,377..378,381,444)
                     /site_type="active"
                     /db_xref="CDD:200493"
     Site            order(155,161..162,164,167..168,175..176,180..181,
                     185..187,438,441)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200493"
     Site            order(228,270,337)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200493"
ORIGIN      
        1 mqtelvnqie vklrkiyqaa yqpaylekml acaenysnnt rgsidtisek nvyliaygds
       61 ifeknkhplq tlneflqeya qdaitdvhll pifpstsddg fsvtdykqid eqlgdwddvq
      121 kmsenfrvml dfvanhmsks sdwfkrfsdn eapynqffie kdsqfdyknv trprtsplfh
      181 kyengkelwt tfsedqldln vrnidclval tdvllfyask qatsirldai gflwktsgtt
      241 cmhlpethei islwrllide lypnlqiite tnvpheenis yfgdgknean mvyqfplppl
      301 vlhtftchdt tklskwaksi sqvsdtatyf nflashdgig mrpatgilsd eeinslvqka
      361 vqnggqvsyk dnadgtqsvy elninygeal qnldedttee lvtkkiiaah silltlqgvp
      421 aiyyhsllgs kndlvgyees ginrrinrek leknqlvhel ktdtyrktif tslkklvqir
      481 rnhtafspfa tqeildlgpd vfaikreseg eciygiinvt shdiskkvaf sgtnllanqp
      541 vtseleltay evvwikkavq