ID   VIOB_ECOLX              Reviewed;         192 AA.
AC   Q9XCW3;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase;
DE            EC=2.3.1.209;
GN   Name=vioB;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC   STRAIN=O7:K1 / VW187;
RX   PubMed=10517601; DOI=10.1099/00221287-145-9-2485;
RA   Marolda C.L., Feldman M.F., Valvano M.A.;
RT   "Genetic organization of the O7-specific lipopolysaccharide biosynthesis
RT   cluster of Escherichia coli VW187 (O7:K1).";
RL   Microbiology 145:2485-2495(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=O7 / G1112;
RX   PubMed=17905981; DOI=10.1128/jb.00777-07;
RA   Wang Y., Xu Y., Perepelov A.V., Qi Y., Knirel Y.A., Wang L., Feng L.;
RT   "Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc
RT   biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli
RT   O7.";
RL   J. Bacteriol. 189:8626-8635(2007).
CC   -!- FUNCTION: Catalyzes the conversion of dTDP-4-amino-4,6-dideoxy-D-
CC       glucose (dTDP-D-Qui4N) to dTDP-4-acetamido-4,6-dideoxy-D-glucose (dTDP-
CC       D-Qui4NAc). {ECO:0000269|PubMed:17905981}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose = CoA +
CC         dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose + H(+);
CC         Xref=Rhea:RHEA:34531, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:68501, ChEBI:CHEBI:68675;
CC         EC=2.3.1.209; Evidence={ECO:0000269|PubMed:17905981};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=142 uM for dTDP-D-Qui4N {ECO:0000269|PubMed:17905981};
CC         KM=554 uM for acetyl-CoA {ECO:0000269|PubMed:17905981};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000269|PubMed:17905981}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF125322; AAD44155.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XCW3; -.
DR   SMR; Q9XCW3; -.
DR   KEGG; ag:AAD44155; -.
DR   BioCyc; MetaCyc:MON-18137; -.
DR   BRENDA; 2.3.1.209; 2026.
DR   SABIO-RK; Q9XCW3; -.
DR   UniPathway; UPA00030; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Lipopolysaccharide biosynthesis; Transferase.
FT   CHAIN           1..192
FT                   /note="dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase"
FT                   /id="PRO_0000424156"
SQ   SEQUENCE   192 AA;  20695 MW;  3D5FCED98526788F CRC64;
     MAYLDEIQLK EMGFKSVGEN VKISDKASFY GCDNISIGNN VRIDDFCVFS AGEGGIDIHD
     YIHIAVYSSI IGKGKVTISD YANISSRVSI YSSNEYYSGN YMSNPVVPSE YTNIHSGTVF
     IGKHVIIGCG SIVLPDVILH EGAAIGALSV VKEDCEAFTV NVGIPAKPIS ERSKKLLELE
     SVFKPSAIGD NL