Q0TCW8 (KBAY_ECOL5) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
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: D-tagatose-1,6-bisphosphate aldolase subunit KbaY Short name=TBPA Short name=TagBP aldolase EC=4.1.2.40 Alternative name(s): D-tagatose-bisphosphate aldolase class II Ketose 1,6-bisphosphate aldolase class II Tagatose-bisphosphate aldolase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 362663 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 286 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stability By similarity. HAMAP MF_01293 |
| Catalytic activity | D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. HAMAP MF_01293 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_01293 |
| Pathway | Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2. HAMAP MF_01293 |
| Subunit structure | Homotetramer. Forms a complex with KbaZ By similarity. HAMAP MF_01293 |
| Sequence similarities | Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase KbaY subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | tagatose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred 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 – 286 | 286 | D-tagatose-1,6-bisphosphate aldolase subunit KbaY HAMAP MF_01293 | PRO_0000355327 | |||||
Regions | |||||||||
| Region | 209 – 211 | 3 | Dihydroxyacetone phosphate binding By similarity | ||||||
| Region | 230 – 233 | 4 | Dihydroxyacetone phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 82 | 1 | Proton donor By similarity | ||||||
| Metal binding | 83 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 180 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 208 | 1 | Zinc; catalytic By similarity | ||||||
| Binding site | 181 | 1 | Dihydroxyacetone phosphate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 536 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000247 Genomic DNA. Translation: ABG71211.1. |
| RefSeq | YP_671112.1. NC_008253.1. |
3D structure databases | |
| ProteinModelPortal | Q0TCW8. |
| SMR | Q0TCW8. Positions 2-284. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0TCW8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000046200; EBESCP00000044389; EBESCG00000045250. |
| GeneID | 4188585. |
| GenomeReviews | Gene locus ECP_3229 in contig CP000247_GR. |
| KEGG | ecp:ECP_3229. |
| PATRIC | 18197304. VBIEscCol77757_3271. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0191. |
| GeneTree | EBGT00050000009021. |
| HOGENOM | HBG327581. |
| OMA | TIELGVC. |
| PhylomeDB | Q0TCW8. |
| ProtClustDB | PRK12738. |
Enzyme and pathway databases | |
| BioCyc | ECOL362663:ECP_3229-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01293. TagBP_aldolase_KbaY. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR000771. Ketose_bisP_aldolase_II. IPR023788. TagBP_ald_KbaY. IPR011288. TagBP_ald_KbaY/GatY. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| KO | K08302. |
| Pfam | PF01116. F_bP_aldolase. 1 hit. [Graphical view] |
| PIRSF | PIRSF001359. F_bP_aldolase_II. 1 hit. |
| TIGRFAMs | TIGR00167. CbbA. 1 hit. TIGR01858. Tag_bisphos_ald. 1 hit. |
| PROSITE | PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KBAY_ECOL5 | ||||||||
| Accession | Primary (citable) accession number: Q0TCW8 | ||||||||
| 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 |

Clusters with