Trimethylamine-N-oxide reductase 1 precursor - Escherichia coli (strain K12)

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P33225 (TORA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	848 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Periplasm
Domain	Signal
Ligand	Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from expression pattern. Source: EcoCyc anaerobic respiration Inferred from expression pattern. Source: EcoCyc
Cellular component	membrane Inferred from Biological aspect of Ancestor. Source: RefGenome periplasmic space Inferred from direct assay Ref.6. Source: EcoCyc
Molecular function	electron carrier activity Inferred from direct assay. Source: EcoCyc molybdenum ion binding Inferred from direct assay. Source: EcoCyc trimethylamine-N-oxide reductase (cytochrome c) activity Inferred from mutant phenotype. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 39

Tat-type signal Ref.1

Chain

40 – 848

809

Trimethylamine-N-oxide reductase 1

PRO_0000019151

Experimental info

Sequence conflict

173

L → R in CAA52095. Ref.1

Sequence conflict

176

A → R in CAA52095. Ref.1

Sequence conflict

256

A → R AA sequence Ref.1

Sequence conflict

258

V → S AA sequence Ref.1

Sequence conflict

281

R → G in CAA52095. Ref.1

Sequence conflict

325

Q → E in CAA52095. Ref.1

Sequence conflict

348

T → S in CAA52095. Ref.1

Sequence conflict

503 – 504

KL → NV in CAA52095. Ref.1

Sequence conflict

713 – 714

QQ → HE in CAA52095. Ref.1

Sequence conflict

751

L → M in CAA52095. Ref.1

Sequence conflict

781

P → L in CAA52095. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P33225 [UniParc].

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

FASTA

848

94,456

        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' referencesShow '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. 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.
[8]	"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G. J. Biol. Chem. 282:8309-8316(2007) [PubMed: 17218314] [Abstract] Cited for: EXPORT VIA THE TAT-SYSTEM.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73888 Genomic DNA. Translation: CAA52095.1. U00096 Genomic DNA. Translation: AAC74082.1. AP009048 Genomic DNA. Translation: BAA36139.1. D16500 Genomic DNA. No translation available.
PIR	C64841.
RefSeq	NP_415517.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P33225.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-11013N.
IntAct	P33225. 13 interactions.
MINT	MINT-6796194.
Protein family/group databases
TCDB	5.A.3.4.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001101; EBESCP00000001101; EBESCG00000000914. EBESCT00000016538; EBESCP00000015829; EBESCG00000015598.
GeneID	946267.
GenomeReviews	Gene locus JW0982 in contig AP009048_GR. Gene locus b0997 in contig U00096_GR.
KEGG	ecj:JW0982. eco:b0997.
PATRIC	32117219. VBIEscCol129921_1033.
Organism-specific databases
EchoBASE	EB1761.
EcoGene	EG11814. torA.
Phylogenomic databases
eggNOG	COG0243.
GeneTree	EBGT00050000008999.
HOGENOM	HBG304064.
OMA	QQYAVGG.
PhylomeDB	P33225.
ProtClustDB	PRK15102.
Enzyme and pathway databases
BioCyc	EcoCyc:TORA-MONOMER.
Gene expression databases
Genevestigator	P33225.
Family and domain databases
InterPro	IPR009010. Asp_de-COase-like_fold. IPR006658. BisC. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006311. TAT_signal. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
KO	K07811.
Pfam	PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR00509. BisC_fam. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. False negative. PS00490. MOLYBDOPTERIN_PROK_2. 1 hit. PS00932. MOLYBDOPTERIN_PROK_3. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TORA_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents