ID   Q18A66_CLOD6            Unreviewed;       185 AA.
AC   Q18A66;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Acetyltransferase {ECO:0000256|RuleBase:RU367021};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU367021};
GN   Name=maa {ECO:0000313|EMBL:CAJ67705.1};
GN   OrderedLocusNames=CD630_08720 {ECO:0000313|EMBL:CAJ67705.1};
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ67705.1, ECO:0000313|Proteomes:UP000001978};
RN   [1] {ECO:0000313|EMBL:CAJ67705.1, ECO:0000313|Proteomes:UP000001978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630 {ECO:0000313|EMBL:CAJ67705.1,
RC   ECO:0000313|Proteomes:UP000001978};
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
RN   [2] {ECO:0007829|PDB:3SRT}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RA   Tan K., Gu M., Peterson S., Anderson W.F., Joachimiak A.;
RT   "The crystal structure of a maltose O-acetyltransferase from Clostridium
RT   difficile 630.";
RL   Submitted (JUL-2011) to the PDB data bank.
RN   [3] {ECO:0007829|PDB:4ISX}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ACETYL-COA.
RA   Tan K., Gu G., Peterson S., Anderson W.F., Joachimiak A.;
RT   "The crystal structure of maltose o-acetyltransferase from clostridium
RT   difficile 630 in complex with acetyl-coa.";
RL   Submitted (JAN-2013) to the PDB data bank.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000256|ARBA:ARBA00007274, ECO:0000256|RuleBase:RU367021}.
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DR   EMBL; AM180355; CAJ67705.1; -; Genomic_DNA.
DR   RefSeq; WP_009888695.1; NZ_JAUPES010000028.1.
DR   RefSeq; YP_001087346.1; NC_009089.1.
DR   PDB; 3SRT; X-ray; 2.50 A; A/B=1-185.
DR   PDB; 4ISX; X-ray; 2.70 A; A/B=1-185.
DR   PDBsum; 3SRT; -.
DR   PDBsum; 4ISX; -.
DR   AlphaFoldDB; Q18A66; -.
DR   SMR; Q18A66; -.
DR   STRING; 272563.CD630_08720; -.
DR   EnsemblBacteria; CAJ67705; CAJ67705; CD630_08720.
DR   KEGG; cdf:CD630_08720; -.
DR   KEGG; pdc:CDIF630_00992; -.
DR   PATRIC; fig|272563.120.peg.896; -.
DR   eggNOG; COG0110; Bacteria.
DR   OrthoDB; 9801697at2; -.
DR   PhylomeDB; Q18A66; -.
DR   BioCyc; PDIF272563:G12WB-980-MONOMER; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03357; LbH_MAT_GAT; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR039369; LacA-like.
DR   InterPro; IPR024688; Mac_dom.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43017:SF1; ACETYLTRANSFERASE YJL218W-RELATED; 1.
DR   PANTHER; PTHR43017; GALACTOSIDE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12464; Mac; 1.
DR   SMART; SM01266; Mac; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3SRT, ECO:0007829|PDB:4ISX};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU367021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001978};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367021}.
FT   DOMAIN          4..58
FT                   /note="Maltose/galactoside acetyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM01266"
FT   BINDING         83
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
FT   BINDING         137
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
FT   BINDING         140
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
FT   BINDING         158
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
FT   BINDING         163
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
FT   BINDING         164
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
FT   BINDING         181
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:4ISX"
SQ   SEQUENCE   185 AA;  20712 MW;  C55FFCCAAA4529EF CRC64;
     MTEKEKMLSG KGYYANDELL VKEREYCKKL TRLFNNTLED EYEKREDILR QLFGSVGKQI
     NVEQNIRCDY GYNIHVGENF FANYDCIFLD VCKIEIGDNV MLAPNVQIYT AYHPIDAQLR
     NSGIEYGSPV KIGDNVWIGG GVIITPGITI GDNVVIGAGS VVTKDIPPNT VAVGNPCRVI
     KKIEE
//