torA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

TorA

Synonyms

trimethylamine N-oxide (TMAO) reductase I, catalytic subunit[1], B0997[2][1], TorA[2][1] , ECK0988, JW0982, b0997

Product description

trimethylamine N-oxide reductase, catalytic subunit[2][3];

Component of trimethylamine N-oxide reductase I[2][3]

Molybdoprotein trimethylamine N-oxide reductase[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0030288

outer membrane-bounded periplasmic space

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0009055

electron carrier activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006655

F

Seeded from EcoCyc (v14.0)

complete

GO:0009055

electron carrier activity

PMID:11056172[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0009060

aerobic respiration

PMID:17850256[6]

IEP: Inferred from Expression Pattern

P

Seeded from EcoCyc (v14.0)

complete

GO:0009061

anaerobic respiration

PMID:17850256[6]

IEP: Inferred from Expression Pattern

P

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006655

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006656

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006657

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006658

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

F

Seeded from EcoCyc (v14.0)

complete

GO:0030151

molybdenum ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006657

F

Seeded from EcoCyc (v14.0)

complete

GO:0030151

molybdenum ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011887

F

Seeded from EcoCyc (v14.0)

complete

GO:0030151

molybdenum ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0500

F

Seeded from EcoCyc (v14.0)

complete

GO:0030151

molybdenum ion binding

PMID:18163615[7]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011887

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0574

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0200

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

PMID:2512991[8]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0050626

trimethylamine-N-oxide reductase (cytochrome c) activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011887

F

Seeded from EcoCyc (v14.0)

complete

GO:0050626

trimethylamine-N-oxide reductase (cytochrome c) activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.7.2.3

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006658

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011887

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

GO:0050626

trimethylamine-N-oxide reductase (cytochrome c) activity

PMID:18522945[9]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005515

protein binding

PMID:11562502[10]

IPI: Inferred from Physical Interaction

EcoliWiki:torC


F

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of trimethylamine N-oxide reductase I

could be indirect

Protein

yibN

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

mutT

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

hns

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

yghW

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

napA

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

tatE

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

groL

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

ybfO

PMID:16606699[11]

Experiment(s):EBI-1138562

Protein

metL

PMID:16606699[11]

Experiment(s):EBI-1138562
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

periplasm

Periplasm

PMID:15073303[12]

EchoLocation:torA


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MNNNDLFQAS RRRFLAQLGG LTVAGMLGPS LLTPRRATAA QAATDAVISK EGILTGSHWG
AIRATVKDGR FVAAKPFELD KYPSKMIAGL PDHVHNAARI RYPMVRVDWL RKRHLSDTSQ
RGDNRFVRVS WDEALDMFYE ELERVQKTHG PSALLTASGW QSTGMFHNAS GMLAKAIALH
GNSVGTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DLLKNQQANW
WCPDHDVYEY YAQLKAKVAA GEIEVISIDP VVTSTHEYLG REHVKHIAVN PQTDVPLQLA
LAHTLYSENL YDKNFLANYC VGFEQFLPYL LGEKDGQPKD AAWAEKLTGI DAETIRGLAR
QMAANRTQII AGWCVQRMQH GEQWAWMIVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK
GVILSGFSGS TSIPPVHDNS DYKGYSSTIP IARFIDAILE PGKVINWNGK SVKLPPLKMC
IFAGTNPFHR HQQINRIIEG LRKLETVIAI DNQWTSTCRF ADIVLPATTQ FERNDLDQYG
NHSNRGIIAM KQVVPPQFEA RNDFDIFREL CRRFNREEAF TEGLDEMGWL KRIWQEGVQQ
GKGRGVHLPA FDDFWNNKEY VEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD
MNYDDCQGHP MWFEKIERSH GGPGSQKYPL HLQSVHPDFR LHSQLCESET LRQQYTVAGK
EPVFINPQDA SARGIRNGDV VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGE
PGALCKYGNP NVLTIDIGTS QLAQATSAHT TLVEIEKYNG TVEQVTAFNG PVEMVAQCEY
VPASQVKS
Length

848

Mol. Wt

94.455 kDa

pI

6.8 (calculated)

Extinction coefficient

150,230 - 151,480 (calc based on 27 Y, 20 W, and 10 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

motif

1-39

UniProt Manual:Signal Peptides

UniProt:P33225

Domain

99..573

PF00384 Molybdopterin oxidoreductase

PMID:19920124[13]

Domain

690..812

PF01568 Molydopterin dinucleotide binding domain

PMID:19920124[13]

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<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=torA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128963

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946267

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0003372

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P33225

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11814

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11814

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946267

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001747

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1761

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Gon, S et al. (2001) Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J. Biol. Chem. 276 11545-51 PubMed
  6. ↑ 6.0 6.1 Ansaldi, M et al. (2007) Aerobic TMAO respiration in Escherichia coli. Mol. Microbiol. 66 484-94 PubMed
  7. ↑ Zhang, L et al. (2008) Structure of the molybdenum site of Escherichia coli trimethylamine N-oxide reductase. Inorg Chem 47 1074-8 PubMed
  8. ↑ Silvestro, A et al. (1989) The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers. Biochim. Biophys. Acta 999 208-16 PubMed
  9. ↑ Genest, O et al. (2008) Dedicated metallochaperone connects apoenzyme and molybdenum cofactor biosynthesis components. J. Biol. Chem. 283 21433-40 PubMed
  10. ↑ Gon, S et al. (2001) An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 98 11615-20 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 11.4 11.5 11.6 11.7 11.8 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ Ilbert, M et al. (2004) Functional and structural analysis of members of the TorD family, a large chaperone family dedicated to molybdoproteins. Microbiology (Reading, Engl.) 150 935-43 PubMed
  13. ↑ 13.0 13.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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