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P58360 (TORA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:Z1415, ECs1152
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

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

General annotation (Comments)

Function

Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions By similarity.

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 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.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMolybdenum
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   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: InterPro

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 Potential
Chain40 – 848809Trimethylamine-N-oxide reductase 1
PRO_0000019153

Sequences

Sequence LengthMass (Da)Tools
P58360 [UniParc].

Last modified November 16, 2001. Version 1.
Checksum: ABFFD02ED178932F

FASTA84894,446
        10         20         30         40         50         60 
MNNNDLFQAS RRRFLAQLGG LTVAGMLGPS LLTSRRATAA QAATEAVISK 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 WRKLETVIAI 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 GGPGSQTYPL HLQSVHPDFR LHSQLCESET LRQQYTVAGK 

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

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


VPASQVKL

« Hide

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. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [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. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG55544.1.
BA000007 Genomic DNA. Translation: BAB34575.1.
PIRD85635.
H90772.
RefSeqNP_286933.1. NC_002655.2.
NP_309179.1. NC_002695.1.

3D structure databases

ProteinModelPortalP58360.
SMRP58360. Positions 58-834.
ModBaseSearch...

Protein-protein interaction databases

STRING155864.Z1415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG55544; AAG55544; Z1415.
BAB34575; BAB34575; BAB34575.
GeneID913030.
959060.
KEGGece:Z1415.
ecs:ECs1152.
PATRIC18351565. VBIEscCol44059_5361.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000284391.
KOK07811.
OMANKDTLHV.
ProtClustDBPRK15102.

Enzyme and pathway databases

BioCycECOL386585:GJFA-1145-MONOMER.

Family and domain databases

Gene3D2.40.40.20. 1 hit.
InterProIPR009010. Asp_de-COase-like_dom.
IPR006658. BisC.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR00509. bisC_fam. 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_ECO57
AccessionPrimary (citable) accession number: P58360
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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