ID   UDG_STRP8               Reviewed;         402 AA.
AC   Q8NKX0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 35.
DE   RecName: Full=UDP-glucose 6-dehydrogenase;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22;
GN   Name=hasB; OrderedLocusNames=spyM18_2237;
OS   Streptococcus pyogenes serotype M18.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232 / Serotype M18;
RX   MEDLINE=21927593; PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA   Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA   Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18
RT   group A Streptococcus strains associated with acute rheumatic fever
RT   outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC   -!- FUNCTION: Catalyzes the formation of UDP-glucuronic acid which is
CC       required for capsular hyaluronic acid synthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP-
CC       glucuronate + 2 NADH.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate
CC       biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; AE010123; AAL98668.1; -; Genomic_DNA.
DR   PIR; A46089; A46089.
DR   HSSP; Q07172; 1DLJ.
DR   SMR; Q8NKX0; 1-402.
DR   GenomeReviews; AE009949_GR; spyM18_2237.
DR   KEGG; spm:spyM18_2237; -.
DR   HOGENOM; Q8NKX0; -.
DR   BioCyc; SPYO186103:SPYM18_2237-MON; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR017476; Nucleotide_sugar_DH.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DHase_C.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
DR   InterPro; IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DHase_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.
DR   PANTHER; PTHR11374; UDPG_MGDP_DH_Creg; 1.
DR   Pfam; PF00984; UDPG_MGDP_dh; 1.
DR   Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR   Pfam; PF03721; UDPG_MGDP_dh_N; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Complete proteome; NAD;
KW   Oxidoreductase.
FT   CHAIN         1    402       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000074058.
FT   NP_BIND       2     19       NAD (Potential).
FT   ACT_SITE    260    260       By similarity.
SQ   SEQUENCE   402 AA;  45483 MW;  DD1869D659F4CA58 CRC64;
     MKIAVAGSGY VGLSLGVLLS LQNEVTIVDI LPSKVDKINN GLSPIQDEYI EYYLKSKQLS
     IKATLDSKAA YKEAELVIIA TPTNYNSRIN YFDTQHVETV IKEVLSVNSH ATLIIKSTIP
     IGFITEMRQK FQTDRIIFSP EFLRESKALY DNLYPSRIIV SCEENDSPKV KADAEKFALL
     LKSAAKKNNV PVLIMGASEA EAVKLFANTY LALRVAYFNE LDTYAESRKL NSHMIIQGIS
     YDDRIGMHYN NPSFGYGGYC LPKDTKQLLA NYNNIPQTLI EAIVSSNNVR KSYIAKQIIN
     VLKEQESPVK VVGVYRLIMK SNSDNFRESA IKDVIDILKS KDIKIIIYEP MLNKLESEDQ
     SVLVNDLENF KKQANIIVTN RYDNELQDVK NKVYSRDIFG RD
//