H2GBE3 (H2GBE3_CORD2) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 12.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Triosephosphate isomerase HAMAP-Rule MF_00147 Short name=TIM HAMAP-Rule MF_00147 EC=5.3.1.1 HAMAP-Rule MF_00147 Alternative name(s): Triose-phosphate isomerase HAMAP-Rule MF_00147 | ||||||
| Gene names |
| ||||||
| Organism | Corynebacterium diphtheriae (strain 241) [Complete proteome] [HAMAP] EMBL AEX44303.1 | ||||||
| Taxonomic identifier | 698966 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › ![]() |
Protein attributes
| Sequence length | 260 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | D-glyceraldehyde 3-phosphate = glycerone phosphate. SAAS SAAS020861 HAMAP-Rule MF_00147 |
| Pathway | Carbohydrate biosynthesis; gluconeogenesis. SAAS SAAS020861 HAMAP-Rule MF_00147 RuleBase RU000517 Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. SAAS SAAS020861 HAMAP-Rule MF_00147 RuleBase RU000517 |
| Subunit structure | Homodimer By similarity. SAAS SAAS020861 HAMAP-Rule MF_00147 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00147. |
| Sequence similarities | Belongs to the triosephosphate isomerase family. HAMAP-Rule MF_00147 RuleBase RU004162 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 Glycolysis RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 Pentose shunt RuleBase RU003527 SAAS SAAS020861 HAMAP-Rule MF_00147 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00147 |
| Molecular function | Isomerase SAAS SAAS020861 HAMAP-Rule MF_00147 RuleBase RU000517 EMBL AEX44303.1 |
| Technical term | Complete proteome |
| 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 100 | 1 | Electrophile By similarity HAMAP-Rule MF_00147 | ||||||
| Active site | 172 | 1 | Proton acceptor By similarity HAMAP-Rule MF_00147 | ||||||
| Binding site | 10 | 1 | Substrate By similarity HAMAP-Rule MF_00147 | ||||||
| Binding site | 12 | 1 | Substrate By similarity HAMAP-Rule MF_00147 | ||||||
Sequences
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References
| [1] | "Pangenomic study of Corynebacterium diphtheriae that provides insights into the genomic diversity of pathogenic isolates from cases of classical diphtheria, endocarditis, and pneumonia." Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R. Jr. Tauch A.J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 241. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP003207 Genomic DNA. Translation: AEX44303.1. |
| RefSeq | YP_005125505.1. NC_016782.1. |
3D structure databases | |
| ProteinModelPortal | H2GBE3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEX44303; AEX44303; CD241_1238. |
| GeneID | 11674151. |
| KEGG | cdp:CD241_1238. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K01803. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00189. UPA00138. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_00147_B. TIM_B. |
| InterPro | IPR013785. Aldolase_TIM. IPR022896. TrioseP_Isoase_bac/euk. IPR000652. Triosephosphate_isomerase. IPR020861. Triosephosphate_isomerase_AS. [Graphical view] |
| PANTHER | PTHR21139. PTHR21139. 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 | H2GBE3_CORD2 | ||||||||
| Accession | Primary (citable) accession number: H2GBE3 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
