Reviewed,
UniProtKB/Swiss-Prot Q1R8Z2 (FCTA_ECOUT)
Last modified
July 13, 2010.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and originHide
| Protein names | Recommended name: Formyl-coenzyme A transferase Short name=Formyl-CoA transferase EC=2.8.3.16 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 364106 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributesHide
| Sequence length | 416 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)Hide
| Function | Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate By similarity. HAMAP MF_00742 |
| Catalytic activity | Formyl-CoA + oxalate = formate + oxalyl-CoA. HAMAP MF_00742 |
| Pathway | Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 1/2. HAMAP MF_00742 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00742 |
| Sequence similarities | Belongs to the caiB/baiF CoA-transferase family. |
OntologiesHide
| Keywords | |
|---|---|
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | formyl-CoA transferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)Hide
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 416 | 416 | Formyl-coenzyme A transferase HAMAP MF_00742 | PRO_0000300987 | |||||
Sites | |||||||||
| Active site | 169 | 1 | Nucleophile By similarity | ||||||
| Binding site | 96 | 1 | Coenzyme A By similarity | ||||||
SequencesHide
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ReferencesHide
| [1] | "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-referencesHide
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000243 Genomic DNA. Translation: ABE08172.1. |
| RefSeq | YP_541703.1. |
3D structure databases | |
| SMR | Q1R8Z2. Positions 1-416. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1R8Z2. |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000070424; EBESCP00000067902; EBESCG00000069471. |
| GeneID | 3989766. |
| GenomeReviews | Gene locus UTI89_C2706 in contig CP000243_GR. |
| KEGG | eci:UTI89_C2706. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1804. |
| HOGENOM | HBG659028. |
| OMA | DEWANDP. |
| ProtClustDB | PRK05398. |
Enzyme and pathway databases | |
| BioCyc | ECOL364106:UTI89_C2706-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00742. Formyl-CoA_transfer. [Tree] |
| InterPro | IPR003673. CoA-Trfase_fam_III. IPR017659. Formyl-CoA_transferase. [Graphical view] |
| Gene3D | G3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit. |
| PANTHER | PTHR11837. CAIB_BAIF. 1 hit. |
| Pfam | PF02515. CoA_transf_3. 1 hit. [Graphical view] |
| SUPFAM | SSF89796. CoA-Trfase_fam_III. 1 hit. |
| TIGRFAMs | TIGR03253. oxalate_frc. 1 hit. |
| ProtoNet | Search... |
Entry informationHide
| Entry name | FCTA_ECOUT | ||||||||
| Accession | Primary (citable) accession number: Q1R8Z2 | ||||||||
| 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 documentsHide
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


