MULTISPECIES: alpha-1,4-glucan--maltose-1-phosphate

LOCUS       WP_003113645             664 aa            linear   BCT 31-DEC-2024
            maltosyltransferase [Pseudomonas].
ACCESSION   WP_003113645
VERSION     WP_003113645.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 664)
  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 664)
  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 664)
  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 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..664
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76199
     Region          20..203
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          208..562
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(261,265,276,278,321,353..354,356..357,391,393..394,
                     422,480,533..534)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(339..341,348..350,363,396..399,401,404,426,428..429,
                     432,436)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(393,422,480)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(425..427,444,447..448)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
ORIGIN      
        1 mssivrnsdd dplviaiqqp riaiesvspv veegaypakt esdrdlrlaa rifadghevl
       61 gaevvwrrvg etaerrlpll pegndfwsaq lrtppcgrly frieawidrf agyrrelrak
      121 hgarlpldle lregdellqr caerggpeia aacaplaerl qacqsveerv alwlaaqtge
      181 llrlvgpreh lvrsreypve verplarfas wyelfprses gdptrhgtfd dvirrlpqia
      241 amgfdvlyfp pihpigrthr kgrnnslrae agdpgspyai gseeggheai hpelgdredf
      301 rrllvavreh gmelaldfai qcspdhpwlr ehpgwfawrp dgslryaenp pkkyedivnv
      361 dfyaeqalps lwealrdvvl gwveqgvtlf rvdnphtkpl pfwewliaev rgrhpqvifl
      421 seaftrpamm arlgkvgfsq sytyftwrnd kqelaeyfae lnqppwrdcy rpnffvntpd
      481 inpwflqrsg rpgfliraal atmgsglwgm ysgfelceaa alpgkeeyld sekyqlrprd
      541 yqapgnivae iarlnrirre npalqthlgf qaynawndri lyfgkrtadl anfvlvavcl
      601 dpheaqeahf elplwefglp ddaslqgedl mnghrwvwhg kvqwmriepw hlpfgiwrvr
      661 rvda