Reviewed,
UniProtKB/Swiss-Prot P96985 (TPIS3_RHIEC)
Last modified
February 9, 2010.
Version 56.
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 |
| ||||
| Organism | Rhizobium etli (strain CFN 42 / ATCC 51251) | ||||
| Taxonomic identifier | 347834 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium |
Protein attributes
| Sequence length | 226 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology. |
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. |
| Sequence similarities | Belongs to the triosephosphate isomerase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis Glycolysis Pentose shunt |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| 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 |
| 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 – ›226 | ›226 | Triosephosphate isomerase HAMAP MF_00147 | PRO_0000090273 | |||||
Sites | |||||||||
| Active site | 91 | 1 | Electrophile By similarity | ||||||
| Active site | 163 | 1 | Proton acceptor By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 226 | 1 | |||||||
Sequences
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References
| [1] | "Evidence that eukaryotic triosephosphate isomerase is of alpha-proteobacterial origin." Keeling P.J., Doolittle W.F. Proc. Natl. Acad. Sci. U.S.A. 94:1270-1275(1997) [PubMed: 9037042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U73964 Genomic DNA. Translation: AAB48823.1. |
3D structure databases | |
| SMR | P96985. Positions 1-226. |
| ModBase | Search... |
Phylogenomic databases | |
| eggNOG | COG0149. |
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 | TPIS3_RHIEC | ||||||||
| Accession | Primary (citable) accession number: P96985 | ||||||||
| 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


