Trimethylamine-N-oxide reductase 1 (P33225)

Identification
Name:Trimethylamine-N-oxide reductase 1
Synonyms:
  • TMAO reductase 1
  • Trimethylamine oxidase 1
Gene Name:torA
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
SMPDB Reactions:
1.0Thumb+3.0Thumb+1.0Thumb+2.0Electron → 1.0Thumb+1.0Thumb+2.0Thumb+1.0menaquinone-8
1.0Trimethylamine N-Oxide + 3.0Hydrogen ion + 1.0Menaquinol 8 + 2.0Electron → 1.0Trimethylamine + 1.0Water + 2.0Hydrogen ion + 1.0menaquinone-8
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Trimethylamine N-Oxide + 1.0NADH + 2.0Hydrogen ion → 1.0Trimethylamine + 1.0NAD + 1.0Water
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Menaquinone 8+1.0Thumb
1.0Hydrogen ion + 1.0Menaquinol 8 + 1.0Trimethylamine N-Oxide → 1.0Water + 1.0Menaquinone 8 + 1.0Trimethylamine
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.02-Demethylmenaquinol 8 + 1.0Hydrogen ion + 1.0Trimethylamine N-Oxide → 1.02-Demethylmenaquinone 8 + 1.0Water + 1.0Trimethylamine
ReactionCard
1.0Thumb+2.0(ferricytochrome c)-subunit+1.0Thumb → 1.0Thumb+2.0(ferrocytochrome c)-subunit+2.0Thumb
1.0Trimethylamine + 2.0(ferricytochrome c)-subunit + 1.0Water → 1.0Trimethylamine N-Oxide + 2.0(ferrocytochrome c)-subunit + 2.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211542-Demethylmenaquinol 8MetaboCard
ECMDB211552-Demethylmenaquinone 8MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00906TrimethylamineMetaboCard
ECMDB04161Trimethylamine N-OxideMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
periplasmic space
Function
binding
catalytic activity
cation binding
electron carrier activity
ion binding
metal ion binding
molybdenum ion binding
oxidoreductase activity
oxidoreductase activity, acting on other nitrogenous compounds as donors
oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor
transition metal ion binding
trimethylamine-N-oxide reductase (cytochrome c) activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0997
Gene OrientationClockwise
Centisome Percentage:22.81
Left Sequence End1058479
Right Sequence End1061025
Gene Sequence:
>2547 bp
ATGAACAATAACGATCTCTTTCAGGCATCACGTCGGCGTTTTCTGGCACAACTCGGCGGC
TTAACCGTCGCCGGGATGCTGGGGCCGTCATTGTTAACGCCGCGACGTGCGACTGCGGCG
CAAGCGGCGACTGACGCTGTCATCTCGAAAGAGGGCATTCTTACCGGGTCGCACTGGGGG
GCTATCCGCGCGACGGTGAAGGATGGTCGCTTTGTGGCGGCAAAACCGTTCGAACTGGAT
AAATATCCGTCGAAAATGATTGCCGGATTGCCGGATCACGTACACAACGCGGCGCGTATT
CGTTATCCGATGGTACGCGTGGACTGGCTGCGTAAGCGCCATCTCAGCGATACCTCCCAG
CGCGGTGATAACCGTTTTGTGCGCGTGAGCTGGGATGAAGCCCTCGACATGTTCTATGAA
GAACTGGAACGCGTGCAGAAAACTCACGGGCCGAGTGCCTTGCTGACCGCCAGTGGTTGG
CAATCGACGGGGATGTTCCATAACGCTTCGGGGATGCTGGCGAAAGCTATTGCCTTGCAT
GGTAATAGCGTTGGTACGGGCGGAGATTACTCTACCGGTGCTGCGCAGGTGATCCTGCCG
CGCGTAGTCGGTTCGATGGAAGTGTATGAACAGCAAACCTCCTGGCCGCTGGTATTGCAG
AACAGCAAAACCATTGTGCTGTGGGGCTCCGATTTGCTGAAAAACCAGCAAGCGAACTGG
TGGTGCCCGGATCACGATGTTTATGAATATTACGCGCAGCTAAAAGCGAAAGTCGCCGCC
GGTGAAATTGAGGTCATCAGCATCGATCCGGTTGTCACATCCACCCATGAGTATCTGGGG
CGCGAGCATGTGAAGCACATTGCGGTTAACCCGCAAACTGACGTGCCGCTGCAACTGGCG
CTGGCACATACGCTGTACAGTGAAAACCTGTACGACAAAAACTTCCTTGCTAACTACTGT
GTGGGTTTTGAGCAGTTCCTGCCGTATCTGCTGGGTGAGAAAGACGGTCAGCCGAAAGAT
GCCGCATGGGCTGAAAAACTGACCGGCATTGATGCCGAAACCATTCGTGGGCTGGCGCGG
CAGATGGCGGCGAACAGAACGCAAATTATTGCTGGCTGGTGCGTGCAGCGTATGCAGCAC
GGTGAACAGTGGGCGTGGATGATTGTGGTTCTGGCGGCGATGCTGGGGCAAATTGGCCTG
CCAGGTGGTGGTTTTGGTTTTGGCTGGCACTACAACGGCGCAGGCACGCCGGGGCGTAAA
GGCGTTATTCTGAGTGGTTTCTCCGGCTCTACGTCGATTCCGCCTGTTCACGACAACAGT
GACTACAAAGGCTACAGCAGCACTATTCCGATTGCCCGTTTTATCGATGCGATCCTCGAA
CCGGGGAAAGTGATCAACTGGAACGGTAAATCGGTAAAACTGCCGCCGCTGAAAATGTGT
ATTTTTGCCGGAACTAACCCATTCCATCGCCATCAGCAGATCAACCGCATTATTGAAGGC
TTGCGCAAGCTGGAAACGGTTATCGCCATAGATAACCAGTGGACCTCAACCTGCCGCTTT
GCCGATATCGTACTGCCTGCGACCACGCAGTTTGAGCGTAACGATCTCGACCAGTACGGC
AATCACTCCAACCGTGGCATTATCGCCATGAAACAGGTGGTGCCGCCGCAGTTCGAGGCG
CGCAACGACTTCGATATTTTCCGCGAGCTGTGCCGTCGCTTTAATCGCGAAGAAGCCTTT
ACCGAAGGGCTGGACGAAATGGGCTGGCTGAAACGCATCTGGCAGGAAGGTGTACAGCAA
GGCAAAGGACGCGGCGTTCATCTGCCAGCGTTTGATGACTTCTGGAATAACAAAGAGTAC
GTCGAGTTTGACCATCCGCAGATGTTTGTTCGCCACCAGGCATTCCGCGAAGATCCGGAT
CTCGAACCGCTGGGCACGCCGAGTGGCCTGATTGAGATCTACTCGAAAACTATCGCCGAT
ATGAACTACGACGATTGTCAGGGGCATCCGATGTGGTTTGAGAAAATCGAACGCTCCCAC
GGTGGGCCTGGCTCGCAAAAGTATCCGTTGCATCTGCAATCTGTGCATCCGGATTTCCGA
CTTCACTCGCAGTTATGTGAGTCGGAAACGCTGCGTCAGCAATATACGGTAGCGGGTAAA
GAGCCAGTATTCATTAACCCGCAGGATGCCAGCGCGCGCGGTATTCGTAACGGTGATGTG
GTACGCGTCTTTAACGCTCGCGGTCAGGTGTTGGCAGGGGCAGTGGTTTCTGACCGCTAT
GCACCCGGCGTGGCACGAATTCACGAAGGGGCATGGTACGATCCAGATAAAGGCGGCGAG
CCTGGTGCGCTGTGCAAATACGGTAACCCCAACGTGTTGACCATCGACATCGGTACATCG
CAGCTGGCGCAGGCGACCAGTGCGCACACTACGCTGGTGGAAATTGAGAAGTACAACGGA
ACAGTGGAGCAGGTGACGGCGTTTAACGGCCCCGTGGAGATGGTGGCGCAGTGCGAATAT
GTTCCCGCGTCGCAGGTGAAATCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:848
Protein Molecular Weight:94455
Protein Theoretical pI:7
Signaling Regions:
  • 1-39
Transmembrane Regions:
  • None
Protein Sequence:
>Trimethylamine-N-oxide reductase 1
MNNNDLFQASRRRFLAQLGGLTVAGMLGPSLLTPRRATAAQAATDAVISKEGILTGSHWG
AIRATVKDGRFVAAKPFELDKYPSKMIAGLPDHVHNAARIRYPMVRVDWLRKRHLSDTSQ
RGDNRFVRVSWDEALDMFYEELERVQKTHGPSALLTASGWQSTGMFHNASGMLAKAIALH
GNSVGTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDLLKNQQANW
WCPDHDVYEYYAQLKAKVAAGEIEVISIDPVVTSTHEYLGREHVKHIAVNPQTDVPLQLA
LAHTLYSENLYDKNFLANYCVGFEQFLPYLLGEKDGQPKDAAWAEKLTGIDAETIRGLAR
QMAANRTQIIAGWCVQRMQHGEQWAWMIVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRK
GVILSGFSGSTSIPPVHDNSDYKGYSSTIPIARFIDAILEPGKVINWNGKSVKLPPLKMC
IFAGTNPFHRHQQINRIIEGLRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQYG
NHSNRGIIAMKQVVPPQFEARNDFDIFRELCRRFNREEAFTEGLDEMGWLKRIWQEGVQQ
GKGRGVHLPAFDDFWNNKEYVEFDHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIAD
MNYDDCQGHPMWFEKIERSHGGPGSQKYPLHLQSVHPDFRLHSQLCESETLRQQYTVAGK
EPVFINPQDASARGIRNGDVVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDPDKGGE
PGALCKYGNPNVLTIDIGTSQLAQATSAHTTLVEIEKYNGTVEQVTAFNGPVEMVAQCEY
VPASQVKS
References
External Links:
ResourceLink
Uniprot ID:P33225
Uniprot Name:TORA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651489
Ecogene ID:EG11814
Ecocyc:EG11814
ColiBase:b0997
Kegg Gene:b0997
EchoBASE ID:EB1761
CCDB:TORA_ECOLI
BacMap:16128963
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Mejean, V., Iobbi-Nivol, C., Lepelletier, M., Giordano, G., Chippaux, M., Pascal, M. C. (1994). "TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon." Mol Microbiol 11:1169-1179. Pubmed: 8022286
  • 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., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "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." DNA Res 3:137-155. Pubmed: 8905232
  • Santini, C. L., Ize, B., Chanal, A., Muller, M., Giordano, G., Wu, L. F. (1998). "A novel sec-independent periplasmic protein translocation pathway in Escherichia coli." EMBO J 17:101-112. Pubmed: 9427745
  • Silvestro, A., Pommier, J., Pascal, M. C., Giordano, G. (1989). "The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers." Biochim Biophys Acta 999:208-216. Pubmed: 2512991
  • Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P., Ribnicky, B., Palmer, T., Georgiou, G. (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282:8309-8316. Pubmed: 17218314
  • Ueguchi, C., Kakeda, M., Yamada, H., Mizuno, T. (1994). "An analogue of the DnaJ molecular chaperone in Escherichia coli." Proc Natl Acad Sci U S A 91:1054-1058. Pubmed: 8302830