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O32271

- TUAD_BACSU

UniProt

O32271 - TUAD_BACSU

Protein

UDP-glucose 6-dehydrogenase TuaD

Gene

tuaD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.

    Catalytic activityi

    UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

    Enzyme regulationi

    Activated by phosphorylation; inhibited by dephosphorylation.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei261 – 2611By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi3 – 2018NADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. NAD binding Source: InterPro
    2. UDP-glucose 6-dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide biosynthetic process Source: InterPro
    2. response to stress Source: UniProtKB-KW
    3. UDP-glucuronate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cell wall biogenesis/degradation, Stress response

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciBSUB:BSU35580-MONOMER.
    RETL1328306-WGS:GSTH-3291-MONOMER.
    UniPathwayiUPA00038; UER00491.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucose 6-dehydrogenase TuaD (EC:1.1.1.22)
    Short name:
    UDP-Glc dehydrogenase
    Short name:
    UDP-GlcDH
    Short name:
    UDPGDH
    Alternative name(s):
    Teichuronic acid biosynthesis protein TuaD
    Gene namesi
    Name:tuaD
    Synonyms:yvhD
    Ordered Locus Names:BSU35580
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU35580. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461UDP-glucose 6-dehydrogenase TuaDPRO_0000074075Add
    BLAST

    Post-translational modificationi

    Phosphorylated by YwqD and dephosphorylated by YwqE in vitro.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO32271.

    PTM databases

    PhosSiteiP0604163.

    Expressioni

    Inductioni

    By phosphate starvation, via the PhoP/PhoR two-component regulatory system.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU35580.

    Structurei

    3D structure databases

    ProteinModelPortaliO32271.
    SMRiO32271. Positions 3-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1004.
    HOGENOMiHOG000153773.
    KOiK00012.
    OMAiVEWARIA.
    OrthoDBiEOG6ZSP7N.
    PhylomeDBiO32271.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR017476. UDP-Glc/GDP-Man.
    IPR014027. UDP-Glc/GDP-Man_DH_C.
    IPR014026. UDP-Glc/GDP-Man_DH_dimer.
    IPR001732. UDP-Glc/GDP-Man_DH_N.
    IPR028357. UDPglc_DH_bac.
    [Graphical view]
    PANTHERiPTHR11374. PTHR11374. 1 hit.
    PfamiPF00984. UDPG_MGDP_dh. 1 hit.
    PF03720. UDPG_MGDP_dh_C. 1 hit.
    PF03721. UDPG_MGDP_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500134. UDPglc_DH_bac. 1 hit.
    PIRSF000124. UDPglc_GDPman_dh. 1 hit.
    SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF52413. SSF52413. 1 hit.
    TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O32271-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIAVIGTG YVGLVSGTCF AEIGNKVVCC DIDESKIRSL KNGVIPIYEP    50
    GLADLVEKNV LDQRLTFTND IPSAIRASDI IYIAVGTPMS KTGEADLTYV 100
    KAAAKTIGEH LNGYKVIVNK STVPVGTGKL VQSIVQKASK GRYSFDVVSN 150
    PEFLREGSAI HDTMNMERAV IGSTSHKAAA IIEELHQPFH APVIKTNLES 200
    AEMIKYAANA FLATKISFIN DIANICERVG ADVSKVADGV GLDSRIGRKF 250
    LKAGIGFGGS CFPKDTTALL QIAKSAGYPF KLIEAVIETN EKQRVHIVDK 300
    LLTVMGSVKG RTISVLGLAF KPNTNDVRSA PALDIIPMLQ QLGAHVKAYD 350
    PIAIPEASAI LGEQVEYYTD VYAAMEDTDA CLILTDWPEV KEMELVKVKT 400
    LLKQPVIIDG RNLFSLEEMQ AAGYIYHSIG RPAVRGTEPS DKYFPGLPLE 450
    ELAKDLGSVN L 461
    Length:461
    Mass (Da):49,816
    Last modified:January 1, 1998 - v1
    Checksum:iF3B4D189FEC90095
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015609 Genomic DNA. Translation: AAB94865.1.
    AL009126 Genomic DNA. Translation: CAB15575.1.
    PIRiF69727.
    RefSeqiNP_391438.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15575; CAB15575; BSU35580.
    GeneIDi936766.
    KEGGibsu:BSU35580.
    PATRICi18979124. VBIBacSub10457_3724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015609 Genomic DNA. Translation: AAB94865.1 .
    AL009126 Genomic DNA. Translation: CAB15575.1 .
    PIRi F69727.
    RefSeqi NP_391438.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O32271.
    SMRi O32271. Positions 3-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU35580.

    PTM databases

    PhosSitei P0604163.

    Proteomic databases

    PaxDbi O32271.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15575 ; CAB15575 ; BSU35580 .
    GeneIDi 936766.
    KEGGi bsu:BSU35580.
    PATRICi 18979124. VBIBacSub10457_3724.

    Organism-specific databases

    GenoListi BSU35580. [Micado ]

    Phylogenomic databases

    eggNOGi COG1004.
    HOGENOMi HOG000153773.
    KOi K00012.
    OMAi VEWARIA.
    OrthoDBi EOG6ZSP7N.
    PhylomeDBi O32271.

    Enzyme and pathway databases

    UniPathwayi UPA00038 ; UER00491 .
    BioCyci BSUB:BSU35580-MONOMER.
    RETL1328306-WGS:GSTH-3291-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR017476. UDP-Glc/GDP-Man.
    IPR014027. UDP-Glc/GDP-Man_DH_C.
    IPR014026. UDP-Glc/GDP-Man_DH_dimer.
    IPR001732. UDP-Glc/GDP-Man_DH_N.
    IPR028357. UDPglc_DH_bac.
    [Graphical view ]
    PANTHERi PTHR11374. PTHR11374. 1 hit.
    Pfami PF00984. UDPG_MGDP_dh. 1 hit.
    PF03720. UDPG_MGDP_dh_C. 1 hit.
    PF03721. UDPG_MGDP_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500134. UDPglc_DH_bac. 1 hit.
    PIRSF000124. UDPglc_GDPman_dh. 1 hit.
    SMARTi SM00984. UDPG_MGDP_dh_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 1 hit.
    SSF52413. SSF52413. 1 hit.
    TIGRFAMsi TIGR03026. NDP-sugDHase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Teichuronic acid operon of Bacillus subtilis 168."
      Soldo B., Lazarevic V., Pagni M., Karamata D.
      Mol. Microbiol. 31:795-805(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Assay for UDPglucose 6-dehydrogenase in phosphate-starved cells: gene tuaD of Bacillus subtilis 168 encodes the UDPglucose 6-dehydrogenase involved in teichuronic acid synthesis."
      Pagni M., Lazarevic V., Soldo B., Karamata D.
      Microbiology 145:1049-1053(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: 168.
    4. "Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases."
      Mijakovic I., Poncet S., Boel G., Maze A., Gillet S., Jamet E., Decottignies P., Grangeasse C., Doublet P., Le Marechal P., Deutscher J.
      EMBO J. 22:4709-4718(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, ENZYME REGULATION.

    Entry informationi

    Entry nameiTUAD_BACSU
    AccessioniPrimary (citable) accession number: O32271
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The nature of the anionic polymer present in the cell wall of B.subtilis depends on phosphate availability. Under phosphate-replete growth conditions teichoic acids are present, whereas under phosphate-depleted conditions, at least part of the wall teichoic acid is replaced with teichuronic acid, a non-phosphate containing anionic polymer. The synthesis of teichuronic acid is accompanied by degradation of teichoic acid and reutilization of liberated phosphate for other cellular processes such as nucleic acid synthesis.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3