ID   YWQF_BACSU              Reviewed;         440 AA.
AC   P96718; Q795B4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-NOV-2008, entry version 60.
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=ywqF; OrderedLocusNames=BSU36230;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98015417; PubMed=9353933;
RA   Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA   Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H.,
RA   Villani G., Kunst F., Danchin A., Glaser P.;
RT   "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT   degrees).";
RL   Microbiology 143:3313-3328(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PHOSPHORYLATION, AND ENZYME REGULATION.
RX   PubMed=12970183; DOI=10.1093/emboj/cdg458;
RA   Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E.,
RA   Decottignies P., Grangeasse C., Doublet P., Le Marechal P.,
RA   Deutscher J.;
RT   "Transmembrane modulator-dependent bacterial tyrosine kinase activates
RT   UDP-glucose dehydrogenases.";
RL   EMBO J. 22:4709-4718(2003).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF TYR-10, AND PHOSPHORYLATION.
RX   PubMed=15741737; DOI=10.1159/000082077;
RA   Mijakovic I., Petranovic D., Deutscher J.;
RT   "How tyrosine phosphorylation affects the UDP-glucose dehydrogenase
RT   activity of Bacillus subtilis YwqF.";
RL   J. Mol. Microbiol. Biotechnol. 8:19-25(2004).
CC   -!- FUNCTION: Catalyzes the conversion of UDP-glucose into UDP-
CC       glucuronate, one of the precursors of teichuronic acid.
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP-
CC       glucuronate + 2 NADH.
CC   -!- ENZYME REGULATION: Competitively inhibited by UDP-glucose.
CC       Activated by phosphorylation, which may increase affinity for
CC       NAD(+); inhibited by dephosphorylation.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate
CC       biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residue(s). Phosphorylated by ywqD
CC       and dephosphorylated by ywqE in vitro.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; Z92952; CAB07444.1; -; Genomic_DNA.
DR   EMBL; Z99122; CAB15640.1; -; Genomic_DNA.
DR   PIR; A70067; A70067.
DR   RefSeq; NP_391504.1; -.
DR   HSSP; P11759; 1MFZ.
DR   PhosSite; P96718; -.
DR   GeneID; 936890; -.
DR   GenomeReviews; AL009126_GR; BSU36230.
DR   KEGG; bsu:BSU36230; -.
DR   NMPDR; fig|224308.1.peg.3630; -.
DR   SubtiList; BG12510; ywqF.
DR   HOGENOM; P96718; -.
DR   BioCyc; BSUB224308:BSU3621-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:EC.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013328; DHase_multihelical.
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:1.10.1040.10; Opine_DH; 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   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; NAD;
KW   Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    440       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000253341.
FT   NP_BIND       2     19       NAD (Potential).
FT   ACT_SITE    260    260       By similarity.
FT   MUTAGEN      10     10       Y->F: 30-fold decrease in activity but no
FT                                decrease in the overall phosphorylation
FT                                level.
SQ   SEQUENCE   440 AA;  47784 MW;  1ADA9454EBE1F645 CRC64;
     MNITVIGTGY VGLVTGVSLS EIGHHVTCID IDAHKIDEMR KGISPIFEPG LEELMRKNTA
     DGRLNFETSY EKGLAQADII FIAVGTPQKS DGHANLEQIT DAAKRIAKHV KRDTVVVTKS
     TVPVGTNDLI NGLITEHLAE PVSISVASNP EFLREGSAIY DTFHGDRIVI GTADEKTANT
     LEELFRPFQI PIYQTDIRSA EMIKYASNAF LATKISFINE ISNICEKVGA DIEAVAYGMG
     QDKRIGSQFL KAGIGYGGSC FPKDTNALVQ IAGNVEHDFE LLKSVIKVNN NQQAMLVDKA
     LNRLGGVTGK TIALLGLSFK PNTDDMREAP SIVIADRLAA LDARIRAYDP IAVSHAKHVL
     PQAVEYKETI EEAVKGSDAV MILTDWADIK QFPLAAYQDL METPLIFDGR NCYTLDEALA
     AGVEYYSVGR KAVVPSGAIQ
//