ID   TUAD_BACSU              Reviewed;         461 AA.
AC   O32271;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
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;
DE   AltName: Full=Teichuronic acid biosynthesis protein tuaD;
GN   Name=tuaD; Synonyms=yvhD; OrderedLocusNames=BSU35580;
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=99157584; PubMed=10048024;
RX   DOI=10.1046/j.1365-2958.1999.01218.x;
RA   Soldo B., Lazarevic V., Pagni M., Karamata D.;
RT   "Teichuronic acid operon of Bacillus subtilis 168.";
RL   Mol. Microbiol. 31:795-805(1999).
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   CHARACTERIZATION.
RC   STRAIN=168;
RX   MEDLINE=99303313; PubMed=10376820;
RA   Pagni M., Lazarevic V., Soldo B., Karamata D.;
RT   "Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene
RT   tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase
RT   involved in teichuronic acid synthesis.";
RL   Microbiology 145:1049-1053(1999).
RN   [4]
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).
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: Activated by phosphorylation; inhibited by
CC       dephosphorylation.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronic acid
CC       biosynthesis; UDP-glucuronic acid from UDP-glucose: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By phosphate starvation, via the phoP/phoR two-
CC       component regulatory system.
CC   -!- PTM: Phosphorylated by ywqD and dephosphorylated by ywqE in vitro.
CC   -!- MISCELLANEOUS: The nature of the anionic polymer present in the
CC       cell wall of B.subtilis depends on phosphate availability. Under
CC       phosphate-replete growth conditions teichoic acids are present,
CC       whereas under phosphate-depleted conditions, at least part of the
CC       wall teichoic acid is replaced with teichuronic acid, a non-
CC       phosphate containing anionic polymer. The synthesis of teichuronic
CC       acid is accompanied by degradation of teichoic acid and
CC       reutilization of liberated phosphate for other cellular processes
CC       such as nucleic acid synthesis.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; AF015609; AAB94865.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15575.1; -; Genomic_DNA.
DR   PIR; F69727; F69727.
DR   RefSeq; NP_391438.1; -.
DR   HSSP; P11759; 1MFZ.
DR   PhosSite; O32271; -.
DR   GeneID; 936766; -.
DR   GenomeReviews; AL009126_GR; BSU35580.
DR   KEGG; bsu:BSU35580; -.
DR   NMPDR; fig|224308.1.peg.3564; -.
DR   SubtiList; BG12691; tuaD.
DR   HOGENOM; O32271; -.
DR   OMA; O32271; CLADVGH.
DR   BioCyc; BSUB224308:BSU3555-MON; -.
DR   BRENDA; 1.1.1.22; 150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD or NADH 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   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR017476; Nucleotide_sugar_DH.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR014028; UDP-Glc/GDP-Man_DH_dimer-bd.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 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.
DR   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; NAD;
KW   Oxidoreductase; Phosphoprotein; Stress response.
FT   CHAIN         1    461       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000074075.
FT   NP_BIND       3     20       NAD (Potential).
FT   ACT_SITE    261    261       By similarity.
SQ   SEQUENCE   461 AA;  49816 MW;  F3B4D189FEC90095 CRC64;
     MKKIAVIGTG YVGLVSGTCF AEIGNKVVCC DIDESKIRSL KNGVIPIYEP GLADLVEKNV
     LDQRLTFTND IPSAIRASDI IYIAVGTPMS KTGEADLTYV KAAAKTIGEH LNGYKVIVNK
     STVPVGTGKL VQSIVQKASK GRYSFDVVSN PEFLREGSAI HDTMNMERAV IGSTSHKAAA
     IIEELHQPFH APVIKTNLES AEMIKYAANA FLATKISFIN DIANICERVG ADVSKVADGV
     GLDSRIGRKF LKAGIGFGGS CFPKDTTALL QIAKSAGYPF KLIEAVIETN EKQRVHIVDK
     LLTVMGSVKG RTISVLGLAF KPNTNDVRSA PALDIIPMLQ QLGAHVKAYD PIAIPEASAI
     LGEQVEYYTD VYAAMEDTDA CLILTDWPEV KEMELVKVKT LLKQPVIIDG RNLFSLEEMQ
     AAGYIYHSIG RPAVRGTEPS DKYFPGLPLE ELAKDLGSVN L
//