Reviewed,
UniProtKB/Swiss-Prot Q81QB5 (IOLD_BACAN)
Last modified
June 16, 2009.
Version 47.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase Short name=THcHDO hydrolase EC=3.7.1.n2 | ||||
| Gene names |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 644 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG) By similarity. |
| Catalytic activity | 3,5/4-trihydroxycyclohexa-1,2-dione + H2O = 5-deoxy-glucuronic acid. HAMAP MF_01669 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity. |
| Pathway | Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 3/7. HAMAP MF_01669 |
| Sequence similarities | Belongs to the TPP enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding NAD Thiamine pyrophosphate |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | inositol catabolic process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: HAMAP thiamin pyrophosphate bindingInferred from electronic annotation. Source: HAMAP transferase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 644 | 644 | 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase HAMAP MF_01669 | PRO_0000352529 | |||||
Regions | |||||||||
| Region | 442 – 522 | 81 | Thiamine pyrophosphate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 493 | 1 | Magnesium By similarity | ||||||
| Metal binding | 520 | 1 | Magnesium By similarity | ||||||
| Binding site | 65 | 1 | Thiamine pyrophosphate By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
| [3] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
Cross-references
Sequence databases | |
|---|---|
| AE016879 Genomic DNA. Translation: AAP26372.1. AE017334 Genomic DNA. Translation: AAT31625.1. AE017225 Genomic DNA. Translation: AAT54647.1. | |
| RefSeq | NP_844886.1. YP_019150.1. YP_028596.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JSC based on UniProtKB P07342. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1085050. 2815665. 2852648. |
| GenomeReviews | Gene locus BA_2514 in contig AE016879_GR. Gene locus BAS2335 in contig AE017225_GR. Gene locus GBAA2514 in contig AE017334_GR. |
| KEGG | ban:BA2514. bar:GBAA2514. bat:BAS2335. |
| TIGR | BA_2514. GBAA_2514. |
Phylogenomic databases | |
| HOGENOM | Q81QB5. |
| OMA | Q81QB5. GELEVYQ. |
Family and domain databases | |
| HAMAP | MF_01669. [Tree] |
| InterPro | IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view] |
| Pfam | PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view] |
| PROSITE | PS00187. TPP_ENZYMES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IOLD_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81QB5 Secondary accession number(s): Q6HYJ2, Q6KSJ3 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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