ID   VIOA_ECOLX              Reviewed;         371 AA.
AC   Q9XCW4;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=dTDP-4-amino-4,6-dideoxy-D-glucose transaminase;
DE            EC=2.6.1.33;
GN   Name=vioA;
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, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   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-dehydro-6-deoxy-D-glucose
CC       (dTDP-D-Glc4O) to dTDP-4-amino-4,6-dideoxy-D-glucose (dTDP-D-Qui4N).
CC       {ECO:0000269|PubMed:17905981}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-D-glucose = dTDP-4-
CC         dehydro-6-deoxy-alpha-D-glucose + L-glutamate; Xref=Rhea:RHEA:19085,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57582,
CC         ChEBI:CHEBI:57649; EC=2.6.1.33;
CC         Evidence={ECO:0000269|PubMed:17905981};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:17905981};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45.8 uM for dTDP-D-Glc4O {ECO:0000269|PubMed:17905981};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000269|PubMed:17905981}.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR   EMBL; AF125322; AAD44154.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XCW4; -.
DR   SMR; Q9XCW4; -.
DR   KEGG; ag:AAD44154; -.
DR   BioCyc; MetaCyc:MON-18136; -.
DR   SABIO-RK; Q9XCW4; -.
DR   UniPathway; UPA00030; -.
DR   GO; GO:0019179; F:dTDP-4-amino-4,6-dideoxy-D-glucose transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR30244; PTHR30244; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Lipopolysaccharide biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..371
FT                   /note="dTDP-4-amino-4,6-dideoxy-D-glucose transaminase"
FT                   /id="PRO_0000424154"
FT   MOD_RES         186
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  41665 MW;  44AA8360C6C630D1 CRC64;
     MNDKTIPVTQ PSLPELAEFM PYLEKIWKNK WLTNNGPFHQ ELEEKLCEFL GVQHISLFNN
     ATIALITALQ ALRITGEVIT TPYSFVATSH AILWNGLTPV FVDIENDGYN IDYRKIEQAI
     TPKTSAILPV HCYSTPCEVE EIQKIADNYG LKVIYDAAHA FGVNFKGGKV YLTMVIYQFL
     VSMRRKSSIN FEGGAIISPD AKTKLRIDRL KNFGIADELT VTAPGINGKM SEINAAFGLV
     QLKHIEGSIS KRKIIDSLYR NLLKGTPGIT IFPGNINTNS NYSYFPILID DGFHMSRDQA
     YELLKKNNIL SRKYFYPLIS NMPMYRGLIS ASVDNLPIAN SVADKVLCLP IYTDLNEEIV
     VKITKLLLGK M