Reviewed,
UniProtKB/Swiss-Prot P33225 (TORA_ECOLI)
Last modified
June 16, 2009.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Trimethylamine-N-oxide reductase 1 Short name=TMAO reductase 1 Short name=Trimethylamine oxidase 1 EC=1.7.2.3 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 848 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. |
| Catalytic activity | Trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+. |
| Cofactor | Molybdenum (molybdopterin) By similarity. |
| Subunit structure | Interacts with the N-terminal domain of torC. |
| Subcellular location | |
| Post-translational modification | Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. |
| Sequence similarities | Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Molybdenum |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion bindingInferred from electronic annotation. Source: UniProtKB-KW trimethylamine-N-oxide reductase (cytochrome c) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 39 | 39 | Tat-type signal Ref.1 | ||||||
| Chain | 40 – 848 | 809 | Trimethylamine-N-oxide reductase 1 | PRO_0000019151 | |||||
Experimental info | |||||||||
| Sequence conflict | 173 | 1 | L → R in CAA52095. Ref.1 | ||||||
| Sequence conflict | 176 | 1 | A → R in CAA52095. Ref.1 | ||||||
| Sequence conflict | 256 | 1 | A → R AA sequence Ref.1 | ||||||
| Sequence conflict | 258 | 1 | V → S AA sequence Ref.1 | ||||||
| Sequence conflict | 281 | 1 | R → G in CAA52095. Ref.1 | ||||||
| Sequence conflict | 325 | 1 | Q → E in CAA52095. Ref.1 | ||||||
| Sequence conflict | 348 | 1 | T → S in CAA52095. Ref.1 | ||||||
| Sequence conflict | 503 – 504 | 2 | KL → NV in CAA52095. Ref.1 | ||||||
| Sequence conflict | 713 – 714 | 2 | QQ → HE in CAA52095. Ref.1 | ||||||
| Sequence conflict | 751 | 1 | L → M in CAA52095. Ref.1 | ||||||
| Sequence conflict | 781 | 1 | P → L in CAA52095. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon." Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M., Pascal M.-C. Mol. Microbiol. 11:1169-1179(1994) [PubMed: 8022286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-46. Strain: K12. |
| [2] | "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T.DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "An analogue of the DnaJ molecular chaperone in Escherichia coli." Ueguchi C., Kakeda M., Yamada H., Mizuno T. Proc. Natl. Acad. Sci. U.S.A. 91:1054-1058(1994) [PubMed: 8302830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 767-848. Strain: K12. |
| [6] | "The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers." Silvestro A., Pommier J., Pascal M.-C., Giordano G. Biochim. Biophys. Acta 999:208-216(1989) [PubMed: 2512991] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [7] | "A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli." Santini C.-L., Ize B., Chanal A., Mueller M., Giordano G., Wu L.-F. EMBO J. 17:101-112(1998) [PubMed: 9427745] [Abstract] Cited for: SEC-INDEPENDENT TRANSLOCATION, PROBABLE EXPORT VIA TAT-SYSTEM. |
Cross-references
Sequence databases | |
|---|---|
| X73888 Genomic DNA. Translation: CAA52095.1. U00096 Genomic DNA. Translation: AAC74082.1. AP009048 Genomic DNA. Translation: BAA36139.1. D16500 Genomic DNA. No translation available. | |
| PIR | C64841. |
| RefSeq | AP_001628.1. NP_415517.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TMO based on UniProtKB O87948. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:11013N. |
Protein family/group databases | |
| TCDB | 5.A.3.4.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family. |
Genome annotation databases | |
| GeneID | 946267. |
| GenomeReviews | Gene locus JW0982 in contig AP009048_GR. Gene locus b0997 in contig U00096_GR. |
| KEGG | ecj:JW0982. eco:b0997. |
Organism-specific databases | |
| EchoBASE | EB1761. |
| EcoGene | EG11814. torA. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P33225. |
| OMA | P33225. LRQQYAV. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:TORA-MON. MetaCyc:TORA-MON. |
Family and domain databases | |
| InterPro | IPR009010. Asp_de-COase-like_fold. IPR006658. BisC. IPR006656. Mopterin_OxRdtase. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006657. MPT_dinuc_bd. IPR006311. Tat. IPR011887. TorA. IPR017909. Twin_arg_translocation_Tat. [Graphical view] |
| Gene3D | G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. |
| Pfam | PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00509. bisC_fam. 1 hit. TIGR01409. TAT_signal_seq. 1 hit. TIGR02164. torA. 1 hit. |
| PROSITE | PS00551. MOLYBDOPTERIN_PROK_1. False negative. PS00490. MOLYBDOPTERIN_PROK_2. 1 hit. PS00932. MOLYBDOPTERIN_PROK_3. 1 hit. PS51318. TAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TORA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P33225 Secondary accession number(s): P78227 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

Clusters with


