Reviewed,
UniProtKB/Swiss-Prot P58362 (TORZ_ECO57)
Last modified
September 22, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Trimethylamine-N-oxide reductase 2 Short name=TMAO reductase 2 Short name=Trimethylamine oxidase 2 EC=1.7.2.3 | ||||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83334 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 809 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N-oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency By similarity. |
| Catalytic activity | Trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+. |
| Cofactor | Molybdenum (molybdopterin) By similarity. |
| Subcellular location | Periplasm By similarity. |
| Post-translational modification | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
| Miscellaneous | Expression of torYZ allows E.coli to grow anaerobically on a wider range of substrates than does expression of torCAD By similarity. |
| 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 |
| 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)
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG56862.1. Different initiation. BA000007 Genomic DNA. Translation: BAB36005.1. Different initiation. | |
| PIR | B85800. F90951. |
| RefSeq | NP_288309.1. NP_310609.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EU1 based on UniProtKB Q57366. |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 5.A.3.4.2. prokaryotic molybdopterin-containing oxidoreductase (PMO) family. |
Genome annotation databases | |
| GeneID | 914087. 961845. |
| GenomeReviews | Gene locus Z2925 in contig AE005174_GR. Gene locus ECs2582 in contig BA000007_GR. |
| KEGG | ece:Z2925. ecs:ECs2582. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P58362. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS2582-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_signal. 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. |
| 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 | TORZ_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P58362 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


