ID   VIOA_SHIDY              Reviewed;         367 AA.
AC   Q6U1I3;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=dTDP-4-amino-4,6-dideoxy-D-glucose transaminase;
DE            EC=2.6.1.33;
GN   Name=vioA;
OS   Shigella dysenteriae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M1354 / Serotype 7;
RX   PubMed=14687563; DOI=10.1016/j.micpath.2003.10.003;
RA   Feng L., Tao J., Guo H., Xu J., Li Y., Rezwan F., Reeves P., Wang L.;
RT   "Structure of the Shigella dysenteriae 7 O antigen gene cluster and
RT   identification of its antigen specific genes.";
RL   Microb. Pathog. 36:109-115(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   PATHWAY.
RC   STRAIN=G1222 / Serotype 7;
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). L-
CC       glutamine can also be used as amino donor.
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=980 uM for dTDP-D-Glc4O {ECO:0000269|PubMed:17905981};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {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; AY380835; AAR97958.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6U1I3; -.
DR   SMR; Q6U1I3; -.
DR   KEGG; ag:AAR97958; -.
DR   SABIO-RK; Q6U1I3; -.
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..367
FT                   /note="dTDP-4-amino-4,6-dideoxy-D-glucose transaminase"
FT                   /id="PRO_0000424155"
FT   MOD_RES         184
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  41407 MW;  020594FED52ED79C CRC64;
     MEKPIFVTQP NLPPLEEFIP YLEIIWQNKQ FTNNGPMHQK LEKKLCEFLG VEYISLFNNG
     TIALITAVQA LGVKGEVITT PYSFVATAHS LVLNGLKPVF VDIDPKTLNI DPRRIEEAIT
     PETQAIMPVH CYGNPCDTQA IADIAQKYNL KVIYDAAHAF GVEDDDGSVL RHGDLSVLSF
     HATKVFSTFE GGAIVCNSKE MKEKIDRLKN FGYIDETNIN IIGSNGKMSE VNAAFGLLQL
     EHMDTFLRGR MNADMFYRQK LKDITGISIV IPSGQKISNF SYFPILVESD FPLSRDELFN
     YLKNQNIFAR RYFYPVIPDF QAYLNVGEVC DVKNAREIAS KVLCLPMHAE LSSDILEYIV
     STIREIK