MULTISPECIES: glucosylglycerate phosphorylase [Escherichia].

LOCUS       WP_000810499             559 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_000810499
VERSION     WP_000810499.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Mukherjee,K., Narindoshvili,T. and Raushel,F.M.
  TITLE     Discovery of a Kojibiose Phosphorylase in Escherichia coli K-12
  JOURNAL   Biochemistry 57 (19), 2857-2867 (2018)
   PUBMED   29684280
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Franceus,J., Pinel,D. and Desmet,T.
  TITLE     Glucosylglycerate Phosphorylase, an Enzyme with Novel Specificity
            Involved in Compatible Solute Metabolism
  JOURNAL   Appl. Environ. Microbiol. 83 (19) (2017)
   PUBMED   28754708
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  :: BlastRule
            Evidence Accession :: NBR011286
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..559
                     /gene="ycjM"
     Protein         1..559
                     /product="glucosylglycerate phosphorylase"
                     /EC_number="2.4.1.352"
                     /calculated_mol_wt=64055
     Region          44..501
                     /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(95,98,133,193,197,227,229..230,233,271,273,337..338,
                     378..379,382,443)
                     /site_type="active"
                     /db_xref="CDD:200493"
     Site            order(152,158..159,161,164..165,172..173,177..178,
                     186..188,437,440)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200493"
     Site            order(229,271,338)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200493"
ORIGIN      
        1 mkqkitdyld eiyggtftat hlqklvtrle sakrlitqrr kkhwdesdvv lityadqfhs
       61 ndlkplptfn qfyhqwlqsi fshvhllpfy pwssddgfsv idyhqvasea gewqdiqqlg
      121 ecshlmfdfv cnhmsaksew fknylqqhpg fedffiavdp qtdlsavtrp ralplltpfq
      181 mrdhstrhlw ttfsddqidl nyrspevlla mvdvllcyla kgaeyvrlda vgfmwkepgt
      241 scihlekthl iikllrsiid nvapgtviit etnvphkdni ayfgagddea hmvyqfslpp
      301 lvlhavqkqn vealcawaqn ltlpssnttw fnflashdgi glnplrgllp eseilelvea
      361 lqqegalvnw knnpdgtrsp yeinvtymda lsrressdee rcarfilaha illsfpgvpa
      421 iyiqsilgsr ndyagveklg ynrainrkky hskeitreln deatlrhavy helsrlitlr
      481 rshnefhpdn nftidtinss vmriprsnad gncltglfnv skniqhvnit nlhgrdlise
      541 vdilgneitl rpwqvmwik