Identification
Name:Trimethylamine-N-oxide reductase 2
Synonyms:
  • TMAO reductase 2
  • Trimethylamine oxidase 2
Gene Name:torZ
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. 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
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Menaquinone 8+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB211542-Demethylmenaquinol 8MetaboCard
ECMDB211552-Demethylmenaquinone 8MetaboCard
ECMDB21207Dimethyl sulfideMetaboCard
ECMDB21208Dimethyl sulfoxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB00906TrimethylamineMetaboCard
ECMDB04161Trimethylamine N-OxideMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
electron carrier activity
ion binding
metal ion binding
molybdenum ion binding
oxidoreductase activity
transition metal ion binding
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b1872
Gene OrientationCounterclockwise
Centisome Percentage:42.08
Left Sequence End1952602
Right Sequence End1955031
Gene Sequence:
>2430 bp
GTGTCGTCGTTGCCCGTTGCTGCCGTCTTACCTGAATTACTTACCGCTCTCGATTGTGCG
CCGCAGGTATTATTAAGTGCGCCGACCGGGGCCGGGAAATCAACCTGGCTGCCGCTGCAA
CTGCTGGCGCATCCCGGCATTAACGGGAAAATTATCCTGCTGGAGCCGCGTCGTCTGGCG
GCGCGTAACGTCGCGCAACGGCTGGCGGAGCTGCTTAACGAAAAGCCAGGCGATACCGTT
GGCTACCGGATGCGTGCGCAAAACTGCGTCGGGCCGAATACCCGCCTGGAAGTGGTTACC
GAAGGCGTGCTGACGCGCATGATCCAGCGTGACCCGGAACTGAGCGGTGTTGGACTGGTG
ATCCTTGATGAATTTCATGAGCGCAGCTTGCAGGCGGATTTGGCGTTGGCGCTGTTACTC
GATGTGCAACAAGGTCTGCGTGATGACCTTAAACTGCTGATTATGTCGGCTACCCTGGAC
AACGACCGCTTGCAGCAAATGCTGCCAGAAGCGCCTGTCGTCATCTCAGAAGGGCGCTCG
TTTCCGGTTGAACGCCGTTATTTACCGCTGCCCGCGCATCAGCGTTTTGACGATGCCGTT
GCGGTAGCCACCGCTGAAATGCTGCGTCAGGAAAGCGGATCATTACTGTTATTTTTACCT
GGCGTCGGAGAAATTCAGCGTGTGCAGGAACAACTGGCTTCGCGCATCGGCAGTGATGTA
TTGCTCTGCCCGCTGTATGGCGCGTTGTCGCTGAACGATCAGCGAAAAGCGATCCTCCCG
GCACCGCAAGGGATGCGCAAAGTGGTGCTGGCGACCAATATTGCTGAAACCAGTTTAACC
ATTGAAGGTATTCGTCTGGTGGTGGATTGTGCCCAGGAGCGTGTGGCGCGTTTTGATCCG
CGCACGGGGCTTACGCGACTGATTACTCAACGCGTTAGCCAGGCATCCATGACGCAGCGT
GCCGGGCGCGCCGGGCGTCTGGAGCCGGGTATCAGCCTGCATTTAATCGCCAAAGAACAA
GCAGAACGCGCCGCGGCGCAAAGTGAACCGGAGATCTTACAAAGCGATCTTTCCGGTTTG
CTGATGGAATTACTGCAATGGGGATGCAGCGATCCGGCGCAGATGAGCTGGCTGGATCAA
CCGCCAGTAGTGAATCTACTGGCCGCGAAACGTCTGTTACAAATGCTGGGGGCACTGGAG
GGTGAACGGCTTAGTGCGCAAGGGCAAAAAATGGCAGCGCTGGGTAACGATCCGCGTTTA
GCGGCAATGCTGGTTAGCGCGAAGAACGACGACGAAGCTGCTACCGCGGCAAAAATTGCC
GCCATTCTCGAAGAGCCGCCACGGATGGGCAATAGTGACCTGGGCGTGGCGTTTTCGCGC
AATCAACCAGCCTGGCAGCAACGTAGTCAGCAACTGTTAAAACGCTTAAACGTACGTGGC
GGTGAGGCAGACAGTTCGCTTATCGCGCCGCTACTTGCCGGGGCGTTTGCCGATCGCATT
GCTCGTCGCCGTGGGCAAGATGGACGCTATCAACTGGCAAACGGCATGGGAGCGATGCTC
GATGCCAACGACGCGCTAAGCCGCCACGAATGGTTGATCGCACCGTTATTATTGCAGGGC
AGCGCCTCGCCGGATGCGCGGATTTTACTGGCGCTGCTGGTCGATATTGATGAGTTAGTA
CAACGCTGCCCGCAGCTGGTACAGCAGTCTGACACTGTGGAGTGGGATGACGCGCAAGGT
ACGCTGAAAGCCTGGCGTCGGCTACAAATCGGTCAGTTGACGGTGAAAGTGCAGCCGCTG
GCGAAACCGTCAGAAGACGAGTTGCATCAGGCGATGCTTAATGGCATCCGTGATAAAGGT
TTAAGCGTGCTCAACTGGACGGCGGAAGCGGAACAGCTACGCTTGCGTTTGTTATGCGCC
GCAAAGTGGTTGCCGGAATATGACTGGCCAGCGGTTGATGATGAAAGTTTATTGGCAGCG
CTGGAAACGTGGCTGCTGCCACATATGACTGGCGTACATTCACTACGCGGCCTGAAATCA
CTCGACATTTATCAGGCACTACGCGGATTACTTGATTGGGGAATGCAGCAACGTCTGGAT
AGTGAATTGCCTGCGCATTACACTGTGCCGACGGGAAGCCGGATCGCCATTCGTTATCAT
GAAGATAACCCGCCCGCGCTGGCGGTGAGAATGCAAGAGATGTTTGGCGAGGCCACCAAT
CCGACGATCGCCCAGGGGCGCGTGCCGCTGGTGCTGGAGTTGCTTTCACCTGCCCAAAGG
CCATTACAAATCACACGAGATTTGAGCGACTTCTGGAAAGGAGCGTACCGTGAGGTGCAA
AAAGAGATGAAAGGGCGTTATCCCAAACATGTCTGGCCGGACGACCCGGCAAATACTGCA
CCGACGCGACGGACGAAAAAGTATTCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:809
Protein Molecular Weight:88964
Protein Theoretical pI:7
Signaling Regions:
  • 1-31
Transmembrane Regions:
  • None
Protein Sequence:
>Trimethylamine-N-oxide reductase 2
MTLTRREFIKHSGIAAGALVVTSAAPLPAWAEEKGGKILTAGRWGAMNVEVKDGKIVSST
GALAKTIPNSLQSTAADQVHTTARIQHPMVRKSYLDNPLQPAKGRGEDTYVQVSWEQALK
LIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLQRYMNLAGGYSGHSGDYSTGAA
QVIMPHVVGSVEVYEQQTSWPLILENSQVVVLWGMNPLNTLKIAWSSTDEQGLEYFHQLK
KSGKPVIAIDPIRSETIEFFDDNATWIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYT
TGYPQFEEYLTGKSDNTPKSAVWAAEITGVPEAQIVKLAELMAANRTMLMAGWGIQRQQY
GEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTRVGGVLPEMSAAIAGHASEAAD
DGGMTAIPVARIVDALENPGGKYQHNGKEQTYPNIKMIWWAGGGNFTHHQDTNRLIKAWQ
KPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGDYSNQHIVPMKQAVAPQFEARN
DFDVFADLAELLKPGGKEIYTEGKDEMAWLKFFYDAAQKGARAQRVTMPMFNAFWQQNKL
IEMRHSEKNEQYVRYGDFRADPVKNALGTPSGKIEIYSKTLEKFGYKDCPAHPTWLAPDE
WKGTADEKQLQLLTAHPAHRLHSQLNYAELRKKYAIADREPITIHTEDAARFGIANGDLV
RVWNKRGQILTGAVVTDGIKKGVVCVHEGAWPDLENGLCKNGSANVLTADIPSSQLANAC
AGNSALVYIEKYTGNAPKLTAFDQPAVQA
References
External Links:
ResourceLink
Uniprot ID:P46923
Uniprot Name:TORZ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674354
Ecogene ID:EG13276
Ecocyc:EG13276
ColiBase:b1872
Kegg Gene:b1872
EchoBASE ID:EB3061
CCDB:TORZ_ECOLI
BacMap:90111350
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
  • del Campillo Campbell, A., Campbell, A. (1996). "Alternative gene for biotin sulfoxide reduction in Escherichia coli K-12." J Mol Evol 42:85-90. Pubmed: 8919859
  • Gon, S., Patte, J. C., Mejean, V., Iobbi-Nivol, C. (2000). "The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli." J Bacteriol 182:5779-5786. Pubmed: 11004177
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • 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