ID   UDG_STRP3               Reviewed;         402 AA.
AC   Q8K5G5; Q877W3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 38.
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=SpyM3_1852, SPs1848;
OS   Streptococcus pyogenes serotype M3.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315 / Serotype M3;
RX   MEDLINE=22133808; PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S.,
RA   Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D.,
RA   Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M.,
RA   Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus:
RT   phage-encoded toxins, the high-virulence phenotype, and clone
RT   emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1 / Serotype M3;
RX   MEDLINE=22683278; PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T.,
RA   Hayashi H., Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a
RT   large-scale genomic rearrangement in invasive strains and new insights
RT   into phage evolution.";
RL   Genome Res. 13:1042-1055(2003).
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; AE014074; AAM80459.1; -; Genomic_DNA.
DR   EMBL; BA000034; BAC64943.1; -; Genomic_DNA.
DR   RefSeq; NP_665656.1; -.
DR   RefSeq; NP_803110.1; -.
DR   HSSP; Q07172; 1DLI.
DR   SMR; Q8K5G5; 1-402.
DR   GeneID; 1010167; -.
DR   GeneID; 1065075; -.
DR   GenomeReviews; BA000034_GR; SPs1848.
DR   GenomeReviews; AE014074_GR; SpyM3_1852.
DR   KEGG; spg:SpyM3_1852; -.
DR   KEGG; sps:SPs1848; -.
DR   HOGENOM; Q8K5G5; -.
DR   BioCyc; SPYO193567:SPS1848-MON; -.
DR   BioCyc; SPYO198466:SPYM3_1852-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_0000074056.
FT   NP_BIND       2     19       NAD (Potential).
FT   ACT_SITE    260    260       By similarity.
FT   VARIANT      61     62       IK -> LQ (in strain: SSI-1).
SQ   SEQUENCE   402 AA;  45470 MW;  E47EA5AC60C5407A CRC64;
     MKIAVAGSGY VGLSLGVLLS LQNEVTIVDI LPSKVDKINN GLSPIQDEYI EYYLKSKQLS
     IKATLDSKAA YKEAELVIIA TPTNYNSRIN YFDTQHVETV IKEVLSVNSH ATLIIKSTIP
     IGFITEMRQK FQTDRIIFSP EFLRESKALY DNLYPSRIIV SCEENDSPKV KADAEKFALL
     LKSAAKKNNV PVLIMGASEA EAVKLFANTY LALRVAYFNE LDTYAESRKL NSHMVIQGIS
     YDDRIGMHYN NPSFGYGGYC LPKDTKQLLA NYNNIPQTLI EAIVSSNNVR KSYIAKQIIN
     VLEEQESPVK VVGVYRLIMK SNSDNFRESA IKDVIDILKS KDIKIIIYEP MLNKLESEDQ
     SVLVNDLENF KKQANIIVTN RYDNELQDVK NKVYSRDIFG RD
//