ID   FDTC_ANETH              Reviewed;         192 AA.
AC   Q6T1W7;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase;
DE            EC=2.3.1.197;
DE   AltName: Full=dTDP-D-Fucp3N acetylase;
GN   Name=fdtC;
OS   Aneurinibacillus thermoaerophilus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=143495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=L420-91T;
RX   PubMed=12740380; DOI=10.1074/jbc.m300858200;
RA   Pfoestl A., Hofinger A., Kosma P., Messner P.;
RT   "Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose in
RT   Aneurinibacillus thermoaerophilus L420-91T.";
RL   J. Biol. Chem. 278:26410-26417(2003).
CC   -!- FUNCTION: Catalyzes the transfer of an acetyl group to dTDP-D-Fucp3N to
CC       form dTDP-D-Fucp3NAc in the biosynthesis of dTDP-3-acetamido-3,6-
CC       dideoxy-alpha-D-galactose, a glycan chain of the S-layer.
CC       {ECO:0000269|PubMed:12740380}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
CC         = CoA + dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactopyranose + H(+);
CC         Xref=Rhea:RHEA:32095, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:63305, ChEBI:CHEBI:63676;
CC         EC=2.3.1.197; Evidence={ECO:0000269|PubMed:12740380};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=66.7 uM for dTDP-D-Fucp3N {ECO:0000269|PubMed:12740380};
CC         KM=61.0 uM for acetyl-CoA {ECO:0000269|PubMed:12740380};
CC         Note=kcat is 2.3 sec(-1) with dTDP-D-Fucp3N as substrate. kcat is 3.1
CC         sec(-1) with acetyl-CoA as substrate.;
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; AY442352; AAS55721.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6T1W7; -.
DR   SMR; Q6T1W7; -.
DR   KEGG; ag:AAS55721; -.
DR   BioCyc; MetaCyc:MON-17006; -.
DR   BRENDA; 2.3.1.197; 344.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 3.
DR   SUPFAM; SSF51161; SSF51161; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..192
FT                   /note="dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-
FT                   N-acetyltransferase"
FT                   /id="PRO_0000421825"
SQ   SEQUENCE   192 AA;  21003 MW;  E950340C38BC4781 CRC64;
     MSSSSETCFV HPNAIVETKK IGNNTRIWAF VHILPQAMIG DNCNICDHCF IENDVFIGNN
     VTVKSGIYIW DGVYIEDNVF LGPNVVFTND VFPRSKVYPE SFGRTIVKKG ASIGANSVIV
     AGNIIGEYAM VGAGSVVTRD IPDYALAYGN PARIKGYVCQ CTSKLKFIDN QAVCQCGKRY
     KYADGIVSQL II