Reviewed,
UniProtKB/Swiss-Prot Q4MQ55 (TPIS_BACCE)
Last modified
February 9, 2010.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Triosephosphate isomerase Short name=TIM EC=5.3.1.1 Alternative name(s): Triose-phosphate isomerase | ||||||
| Gene names |
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| Organism | Bacillus cereus | ||||||
| Taxonomic identifier | 1396 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 251 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147 |
| Pathway | Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147 Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00147 |
| Subcellular location | Cytoplasm Probable HAMAP MF_00147. |
| Induction | By salt stress and heat shock. Ref.3 |
| Sequence similarities | Belongs to the triosephosphate isomerase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis Glycolysis Pentose shunt Stress response |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: HAMAP glycolysisInferred from electronic annotation. Source: HAMAP pentose-phosphate shuntInferred from electronic annotation. Source: HAMAP response to stressInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | triose-phosphate isomerase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 251 | 251 | Triosephosphate isomerase HAMAP MF_00147 | PRO_0000271233 | |||||
Sites | |||||||||
| Active site | 95 | 1 | Electrophile By similarity | ||||||
| Active site | 167 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 9 | 1 | Substrate By similarity | ||||||
| Binding site | 11 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 213 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax." Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., Peterson S.N., Weyant R.S. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004) [PubMed: 15155910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G9241. |
| [2] | Nishizawa M., Itoi Y., Ito S., Inoue M. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141. Strain: Tim-r01. |
| [3] | "Heat and salt stress in the food pathogen Bacillus cereus." Browne N., Dowds B.C.A. J. Appl. Microbiol. 91:1085-1094(2001) [PubMed: 11851817] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, INDUCTION. Strain: NCIMB 11796 / DSM 626. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAEK01000016 Genomic DNA. Translation: EAL14302.1. Different initiation. AB083542 Genomic DNA. Translation: BAB88970.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2BTM based on UniProtKB P00943. |
| SMR | Q4MQ55. Positions 2-249. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 5.3.1.1. 604. |
Family and domain databases | |
| HAMAP | MF_00147_B. TIM_B. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR000652. Triosephosphate_isomerase. IPR020861. Triosephosphate_isomerase_AS. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| PANTHER | PTHR21139. Triophos_ismrse. 1 hit. |
| Pfam | PF00121. TIM. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00419. tim. 1 hit. |
| PROSITE | PS00171. TIM_1. 1 hit. PS51440. TIM_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TPIS_BACCE | ||||||||
| Accession | Primary (citable) accession number: Q4MQ55 Secondary accession number(s): P83069, Q8RQH4 | ||||||||
| 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 |

Clusters with


