sugar O-acetyltransferase [Enterovibrio norvegicus].

LOCUS       WP_017003990             185 aa            linear   BCT 25-MAR-2023
ACCESSION   WP_017003990
VERSION     WP_017003990.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio norvegicus
  ORGANISM  Enterovibrio norvegicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Enterovibrio.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
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 10129706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Enterovibrio norvegicus"
                     /db_xref="taxon:188144"
     Protein         1..185
                     /product="sugar O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19423
     Region          12..181
                     /region_name="LbH_MAT_GAT"
                     /note="Maltose O-acetyltransferase (MAT) and Galactoside
                     O-acetyltransferase (GAT): MAT and GAT catalyze the
                     CoA-dependent acetylation of the 6-hydroxyl group of their
                     respective sugar substrates. MAT acetylates maltose and
                     glucose exclusively at the C6...; cd03357"
                     /db_xref="CDD:100047"
     Site            order(15,24,69,81,83,89,91,101,103,109,111,116,118,
                     123..124,126,138,140..141,146,158..159,162,164..165,
                     174..177,179)
                     /site_type="active"
                     /db_xref="CDD:100047"
     Site            order(15,24,69,81,83,89,91,101,111,116,123..124,126)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100047"
     Site            order(25,28,32,39,65,67..68,84..85,99,101,105,107,109,116,
                     118..120,127,129,136,138,141..143,146,154,156,159..160,
                     164,176)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100047"
     Site            order(109,111,116,118,138,140..141,146,158..159,164..165,
                     174..175,177)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100047"
ORIGIN      
        1 mtefekmqqg kpyspadtel tqfryasrrl cqqlnnidpa dadaqdmvvt klfairgkgl
       61 aveapftcty gmnihignnv aigpnctlid sghieignnv ligpgvgiys itqsllpldv
      121 qngeheislp iiignnvvig gnsvikagvs igegvvveag svvdgdiepf avvagnpaav
      181 irrlr