Q59182 (TPIS_BORBU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 77.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | Borrelia burgdorferi (Lyme disease spirochete) | ||||||
| Taxonomic identifier | 139 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group |
Protein attributes
| Sequence length | 253 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147_B |
| Pathway | Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147_B Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147_B |
| Subunit structure | Homodimer By similarity. HAMAP MF_00147_B |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00147_B. |
| Sequence similarities | Belongs to the triosephosphate isomerase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis Glycolysis Pentose shunt |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW glycolysisInferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shuntInferred 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: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 253 | 253 | Triosephosphate isomerase HAMAP MF_00147_B | PRO_0000090184 | |||||
Sites | |||||||||
| Active site | 96 | 1 | Electrophile By similarity | ||||||
| Active site | 169 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 9 | 1 | Substrate By similarity | ||||||
| Binding site | 11 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 201 | 1 | S → T in AAB53932. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii." Anda P., Gebbia J.A., Backenson P.B., Coleman J.L., Benach J.L. Infect. Immun. 64:262-268(1996) [PubMed: 8557349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680. |
| [2] | "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. Venter J.C.Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680. |
| [3] | "Conservation of gene arrangement and an unusual organization of rRNA genes in the linear chromosomes of the Lyme disease spirochaetes Borrelia burgdorferi, B. garinii and B. afzelii." Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G. Microbiology 140:2931-2940(1994) [PubMed: 7812434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74. Strain: 212. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U28760 Genomic DNA. Translation: AAB53932.1. AE000783 Genomic DNA. Translation: AAC66452.1. L32595 Genomic DNA. Translation: AAC41406.1. |
| PIR | G70106. |
| RefSeq | NP_212189.1. NC_001318.1. |
3D structure databases | |
| ProteinModelPortal | Q59182. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBORT00000009137; EBBORP00000008467; EBBORG00000009136. |
| GeneID | 1194891. |
| GenomeReviews | Gene locus BB_0055 in contig AE000783_GR. |
| KEGG | bbu:BB0055. |
| NMPDR | fig|224326.1.peg.439. |
| PATRIC | 20556715. VBIBorBur75917_0453. |
| TIGR | BB_0055. |
Phylogenomic databases | |
| GeneTree | EBGT00050000007284. |
| HOGENOM | HBG708281. |
| OMA | VCVGETQ. |
| PhylomeDB | Q59182. |
| ProtClustDB | PRK00042. |
Enzyme and pathway databases | |
| BioCyc | BBUR224326:BB_0055-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00147_B. TIM_B. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR022896. TrioseP_Isoase_bac/euk. IPR000652. Triosephosphate_isomerase. IPR020861. Triosephosphate_isomerase_AS. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| KO | K01803. |
| PANTHER | PTHR21139. Triophos_ismrse. 1 hit. |
| Pfam | PF00121. TIM. 1 hit. [Graphical view] |
| SUPFAM | SSF51351. Triophos_ismrse. 1 hit. |
| 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_BORBU | ||||||||
| Accession | Primary (citable) accession number: Q59182 Secondary accession number(s): Q59187 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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