Reviewed,
UniProtKB/Swiss-Prot P96718 (YWQF_BACSU)
Last modified
November 25, 2008.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: UDP-glucose 6-dehydrogenase Short name=UDP-Glc dehydrogenase Short name=UDP-GlcDH Short name=UDPGDH EC=1.1.1.22 | ||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 440 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid. |
| Catalytic activity | UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH. |
| Enzyme regulation | Competitively inhibited by UDP-glucose. Activated by phosphorylation, which may increase affinity for NAD(+); inhibited by dephosphorylation. |
| Pathway | |
| Subcellular location | CytoplasmBy similarity. |
| Post-translational modification | Phosphorylated on tyrosine residue(s). Phosphorylated by ywqD and dephosphorylated by ywqE in vitro. |
| Sequence similarities | Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 440 | 440 | UDP-glucose 6-dehydrogenase | PRO_0000253341 | |||||
Regions | |||||||||
| Nucleotide binding | 2 – 19 | 18 | NAD Potential | ||||||
Sites | |||||||||
| Active site | 260 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 10 | 1 | Y → F: 30-fold decrease in activity but no decrease in the overall phosphorylation level | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed: 9353933] [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. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "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: 12970183] [Abstract] Cited for: PHOSPHORYLATION, ENZYME REGULATION. |
| [4] | "How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF." Mijakovic I., Petranovic D., Deutscher J. J. Mol. Microbiol. Biotechnol. 8:19-25(2004) [PubMed: 15741737] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-10, PHOSPHORYLATION. |
Cross-references
Sequence databases | |
|---|---|
| Z92952 Genomic DNA. Translation: CAB07444.1. Z99122 Genomic DNA. Translation: CAB15640.1. | |
| PIR | A70067. |
| RefSeq | NP_391504.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MFZ based on UniProtKB P11759. |
| ModBase | Search... |
PTM databases | |
| PhosSite | P96718. |
Genome annotation databases | |
| GeneID | 936890. |
| GenomeReviews | Gene locus BSU36230 in contig AL009126_GR. |
| KEGG | bsu:BSU36230. |
| NMPDR | fig|224308.1.peg.3630. |
Organism-specific databases | |
| SubtiList | BG12510. ywqF. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P96718. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3621-MON. |
Family and domain databases | |
| InterPro | IPR013328. DHase_multihelical. IPR016040. NAD(P)-bd. IPR017476. Nucleotide_sugar_DH. IPR014027. UDP-Glc/GDP-Man_DHase_C. IPR014026. UDP-Glc/GDP-Man_DHase_dimer. IPR014028. UDP-Glc/GDP-Man_DHase_dimer-bd. IPR001732. UDP-Glc/GDP-Man_DHase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| PANTHER | PTHR11374. UDPG_MGDP_DH_Creg. 1 hit. |
| Pfam | PF00984. UDPG_MGDP_dh. 1 hit. PF03720. UDPG_MGDP_dh_C. 1 hit. PF03721. UDPG_MGDP_dh_N. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | YWQF_BACSU | ||||||||
| Accession | Primary (citable) accession number: P96718 Secondary accession number(s): Q795B4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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