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O32271

- TUAD_BACSU

UniProt

O32271 - TUAD_BACSU

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Protein
UDP-glucose 6-dehydrogenase TuaD
Gene
tuaD, yvhD, BSU35580
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 – 2611 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi3 – 2018NAD Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461UDP-glucose 6-dehydrogenase TuaD
PRO_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.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU35580.

Structurei

3D structure databases

ProteinModelPortaliO32271.
SMRiO32271. Positions 3-430.

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 102 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

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