Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

maltose O-acetyltransferase [Escherichia coli].


LOCUS       WP_000102553             183 aa            linear   BCT 18-JAN-2020
ACCESSION   WP_000102553
VERSION     WP_000102553.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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 :: NF007499.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10092
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..183
                     /gene="maa"
     Protein         1..183
                     /product="maltose O-acetyltransferase"
                     /EC_number="2.3.1.79"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19981
     Region          1..183
                     /region_name="PRK10092"
                     /note="maltose O-acetyltransferase; Provisional"
                     /db_xref="CDD:182235"
     Site            order(16,25,69,81,83,89,91,101,103,109,111,113,115,
                     122..123,125,137,139..140,145,157..158,161,163..164,
                     173..176,178)
                     /site_type="active"
                     /db_xref="CDD:100047"
     Site            order(16,25,69,81,83,89,91,101,111,113,122..123,125)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100047"
     Site            order(26,29,33,40,65,67..68,84..85,99,101,105,107,109,113,
                     115..117,119..120,126,128,135,137,140..142,145,153,155,
                     158..159,163,175)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100047"
     Site            order(109,111,113,115,137,139..140,145,157..158,163..164,
                     173..174,176)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100047"
ORIGIN      
        1 mstekekmia gelyrsadet lsrdrlrarq lihrynhsla eehtlrqqil adlfgqvtea
       61 yieptfrcdy gyniflgnnf fanfdcvmld vcpirigdnc mlalgvhiyt athpidpvar
      121 nsgaelgkpv tignnvwigg ravinpgvti gdnvvvasga vvtkdvpdnv vvggnparii
      181 kkl