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Reviewed, UniProtKB/Swiss-Prot P33225 (TORA_ECOLI)

Last modified June 16, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trimethylamine-N-oxide reductase 1
      Short name=TMAO reductase 1
      Short name=Trimethylamine oxidase 1
    EC=1.7.2.3
Gene names
Name: torA
Ordered Locus Names: b0997, JW0982
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length848 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Periplasm. Ref.6

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 componentPeriplasm
   DomainSignal
   LigandMolybdenum
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

molybdenum ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

trimethylamine-N-oxide reductase (cytochrome c) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939Tat-type signal Ref.1
Chain40 – 848809Trimethylamine-N-oxide reductase 1
PRO_0000019151

Experimental info

Sequence conflict1731L → R in CAA52095. Ref.1
Sequence conflict1761A → R in CAA52095. Ref.1
Sequence conflict2561A → R AA sequence Ref.1
Sequence conflict2581V → S AA sequence Ref.1
Sequence conflict2811R → G in CAA52095. Ref.1
Sequence conflict3251Q → E in CAA52095. Ref.1
Sequence conflict3481T → S in CAA52095. Ref.1
Sequence conflict503 – 5042KL → NV in CAA52095. Ref.1
Sequence conflict713 – 7142QQ → HE in CAA52095. Ref.1
Sequence conflict7511L → M in CAA52095. Ref.1
Sequence conflict7811P → L in CAA52095. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33225-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 59DDACB00B1843E7

FASTA84894,456
        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 

« Hide

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. expand/collapse author list , 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.
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.
PIRC64841.
RefSeqAP_001628.1.
NP_415517.1.

3D structure databases

HSSPHSSP built from PDB template 1TMO based on UniProtKB O87948.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:11013N.

Protein family/group databases

TCDB5.A.3.4.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.

Genome annotation databases

GeneID946267.
GenomeReviewsGene locus JW0982 in contig AP009048_GR.
Gene locus b0997 in contig U00096_GR.
KEGGecj:JW0982.
eco:b0997.

Organism-specific databases

EchoBASEEB1761.
EcoGeneEG11814. torA.
CMRSearch...

Phylogenomic databases

HOGENOMP33225.
OMAP33225. LRQQYAV.

Enzyme and pathway databases

BioCycEcoCyc:TORA-MON.
MetaCyc:TORA-MON.

Family and domain databases

InterProIPR009010. 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]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
PfamPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR00509. bisC_fam. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
TIGR02164. torA. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. False negative.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTORA_ECOLI
AccessionPrimary (citable) accession number: P33225
Secondary accession number(s): P78227
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents