LOCUS WP_371077491 176 aa linear BCT 22-AUG-2024
DEFINITION MULTISPECIES: sugar O-acetyltransferase [unclassified
Sinorhizobium].
ACCESSION WP_371077491
VERSION WP_371077491.1
KEYWORDS RefSeq.
SOURCE unclassified Sinorhizobium
ORGANISM unclassified Sinorhizobium
Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
Sinorhizobium.
REFERENCE 1 (residues 1 to 176)
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..176
/organism="unclassified Sinorhizobium"
/db_xref="taxon:2613772"
Protein 1..176
/product="sugar O-acetyltransferase"
/EC_number="2.3.1.-"
/GO_function="GO:0016407 - acetyltransferase activity
[Evidence IEA]"
/calculated_mol_wt=18473
Region 6..173
/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(9,18,63,75,77,83,85,95,97,103,105,107,109,116..117,
119,131,133..134,139,151..152,155,157..158,167..170,172)
/site_type="active"
/db_xref="CDD:100047"
Site order(9,18,63,75,77,83,85,95,105,107,116..117,119)
/site_type="other"
/note="substrate binding site [chemical binding]"
/db_xref="CDD:100047"
Site order(19,22,26,33,59,61..62,78..79,93,95,99,101,103,107,
109..111,113..114,120,122,129,131,134..136,139,147,149,
152..153,157,169)
/site_type="other"
/note="trimer interface [polypeptide binding]"
/db_xref="CDD:100047"
Site order(103,105,107,109,131,133..134,139,151..152,157..158,
167..168,170)
/site_type="other"
/note="CoA binding site [chemical binding]"
/db_xref="CDD:100047"
ORIGIN
1 maagqwyccl dpeldalrrq ariavhqhnt qppdergnia palralfaet aadvfieapf
61 hcsygmnivl gervylnagc tildsagvri gnasmlgpgv qiycaehhkd pvlrkagmei
121 arpveigdhv wiggraiilg gvkigncaiv gagavvtkdv pagatvvgsp arvmvr
//