[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-46. STRAIN=K12; PubMed=8022286 [NCBI, ExPASy, EBI, Israel, Japan] Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M., Pascal M.-C.; "TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon."; Mol. Microbiol. 11:1169-1179(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] 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., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.; "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(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 767-848. STRAIN=K12; PubMed=8302830 [NCBI, ExPASy, EBI, Israel, Japan] Ueguchi C., Kakeda M., Yamada H., Mizuno T.; "An analogue of the DnaJ molecular chaperone in Escherichia coli."; Proc. Natl. Acad. Sci. U.S.A. 91:1054-1058(1994).
[6]	SUBCELLULAR LOCATION. DOI=10.1016/0167-4838(89)90220-3; PubMed=2512991 [NCBI, ExPASy, EBI, Israel, Japan] Silvestro A., Pommier J., Pascal M.-C., Giordano G.; "The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers."; Biochim. Biophys. Acta 999:208-216(1989).
[7]	SEC-INDEPENDENT TRANSLOCATION, AND PROBABLE EXPORT VIA TAT-SYSTEM. DOI=10.1093/emboj/17.1.101; PubMed=9427745 [NCBI, ExPASy, EBI, Israel, Japan] Santini C.-L., Ize B., Chanal A., Mueller M., Giordano G., Wu L.-F.; "A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli."; EMBO J. 17:101-112(1998).

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: Interacts with the N-terminal domain of torC.
SUBCELLULAR LOCATION: Periplasm.
PTM: Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X73888; CAA52095.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74082.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA36139.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16500; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

C64841; C64841.

RefSeq

AP_001628.1; -.
NP_415517.1; -.

3D structure databases

HSSP

O87948; 1TMO. [HSSP ENTRY / PDB]

ModBase

P33225.

Protein-protein interaction databases

DIP

DIP:11013N; -.

IntAct

P33225; -.

Enzyme and pathway databases

BioCyc

EcoCyc:TORA-MON; -.
MetaCyc:TORA-MON; -.

Organism-specific databases

EchoBASE

EB1761; -.

EcoGene

EG11814; torA.

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.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.

Pfam

PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00509; bisC_fam; 1.
TIGR01409; TAT_signal_seq; 1.
TIGR02164; torA; 1.

PROSITE

PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
PS00490; MOLYBDOPTERIN_PROK_2; 1.
PS00932; MOLYBDOPTERIN_PROK_3; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P33225.

Genome annotation databases

GeneID

946267; -.

GenomeReviews

U00096_GR; b0997.
AP009048_GR; JW0982.

KEGG

ecj:JW0982; -.
eco:b0997; -.

Phylogenomic databases

HOGENOM

P33225; -.

Genome annotation databases

CMR

P33225; b0997.

Other

ProtoNet

P33225.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; Molybdenum; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 39`	`39`	`Tat-type signal.`
`CHAIN`	`40 848`	`809`	`Trimethylamine-N-oxide reductase 1.`	`PRO_0000019151`
`CONFLICT`	`173 173`		`L -> R (in Ref. 1; CAA52095).`
`CONFLICT`	`176 176`		`A -> R (in Ref. 1; CAA52095).`
`CONFLICT`	`256 256`		`A -> R (in Ref. 1; AA sequence).`
`CONFLICT`	`258 258`		`V -> S (in Ref. 1; AA sequence).`
`CONFLICT`	`281 281`		`R -> G (in Ref. 1; CAA52095).`
`CONFLICT`	`325 325`		`Q -> E (in Ref. 1; CAA52095).`
`CONFLICT`	`348 348`		`T -> S (in Ref. 1; CAA52095).`
`CONFLICT`	`503 504`		`KL -> NV (in Ref. 1; CAA52095).`
`CONFLICT`	`713 714`		`QQ -> HE (in Ref. 1; CAA52095).`
`CONFLICT`	`751 751`		`L -> M (in Ref. 1; CAA52095).`
`CONFLICT`	`781 781`		`P -> L (in Ref. 1; CAA52095).`

Sequence information

Length: 848 AA [This is the length of the unprocessed precursor]

Molecular weight: 94456 Da [This is the MW of the unprocessed precursor]

CRC64: 59DDACB00B1843E7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNNNDLFQAS RRRFLAQLGG LTVAGMLGPS LLTPRRATAA QAATDAVISK EGILTGSHWG 

        70         80         90        100        110        120 
AIRATVKDGR FVAAKPFELD KYPSKMIAGL PDHVHNAARI RYPMVRVDWL RKRHLSDTSQ 

       130        140        150        160        170        180 
RGDNRFVRVS WDEALDMFYE ELERVQKTHG PSALLTASGW QSTGMFHNAS GMLAKAIALH 

       190        200        210        220        230        240 
GNSVGTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DLLKNQQANW 

       250        260        270        280        290        300 
WCPDHDVYEY YAQLKAKVAA GEIEVISIDP VVTSTHEYLG REHVKHIAVN PQTDVPLQLA 

       310        320        330        340        350        360 
LAHTLYSENL YDKNFLANYC VGFEQFLPYL LGEKDGQPKD AAWAEKLTGI DAETIRGLAR 

       370        380        390        400        410        420 
QMAANRTQII AGWCVQRMQH GEQWAWMIVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK 

       430        440        450        460        470        480 
GVILSGFSGS TSIPPVHDNS DYKGYSSTIP IARFIDAILE PGKVINWNGK SVKLPPLKMC 

       490        500        510        520        530        540 
IFAGTNPFHR HQQINRIIEG LRKLETVIAI DNQWTSTCRF ADIVLPATTQ FERNDLDQYG 

       550        560        570        580        590        600 
NHSNRGIIAM KQVVPPQFEA RNDFDIFREL CRRFNREEAF TEGLDEMGWL KRIWQEGVQQ 

       610        620        630        640        650        660 
GKGRGVHLPA FDDFWNNKEY VEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD 

       670        680        690        700        710        720 
MNYDDCQGHP MWFEKIERSH GGPGSQKYPL HLQSVHPDFR LHSQLCESET LRQQYTVAGK 

       730        740        750        760        770        780 
EPVFINPQDA SARGIRNGDV VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGE 

       790        800        810        820        830        840 
PGALCKYGNP NVLTIDIGTS QLAQATSAHT TLVEIEKYNG TVEQVTAFNG PVEMVAQCEY 


VPASQVKS

P33225 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools