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Reviewed, UniProtKB/Swiss-Prot O87948 (TORA_SHEMA)

Last modified June 16, 2009. Version 58. 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

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Names and origin

Protein namesRecommended name:
    Trimethylamine-N-oxide reductase
      Short name=TMAO reductase
      Short name=Trimethylamine oxidase
    EC=1.7.2.3
Gene names
Name: torA
OrganismShewanella massilia
Taxonomic identifier76854 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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Protein attributes

Sequence length829 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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+.

Subcellular location

Periplasm.

Induction

By TMAO and DMSO. Ref.1

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Miscellaneous

Although torA is induced by both TMAO and DMSO, only TMAO is used as a natural substrate.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMolybdenum
   Molecular functionOxidoreductase
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131Tat-type signal Ref.1
Chain32 – 829798Trimethylamine-N-oxide reductase
PRO_0000019157

Secondary structure

1 ........................................................................................................................................................ 829
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O87948-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6F58A59E8C41CF1F

FASTA82992,362
        10         20         30         40         50         60 
MNRRDFLKGI ASSSFVVLGG SSVLTPLNAL AKAGINEDEW LTTGSHFGAF KMKRKNGVIA 

        70         80         90        100        110        120 
EVKPFDLDKY PTDMINGIRG MVYNPSRVRY PMVRLDFLLK GHKSNTHQRG DFRFVRVTWD 

       130        140        150        160        170        180 
KALTLFKHSL DEVQTQYGPS GLHAGQTGWR ATGQLHSSTS HMQRAVGMHG NYVKKIGDYS 

       190        200        210        220        230        240 
TGAGQTILPY VLGSTEVYAQ GTSWPLILEH SDTIVLWSND PYKNLQVGWN AETHESFAYL 

       250        260        270        280        290        300 
AQLKEKVKQG KIRVISIDPV VTKTQAYLGC EQLYVNPQTD VTLMLAIAHE MISKKLYDDK 

       310        320        330        340        350        360 
FIQGYSLGFE EFVPYVMGTK DGVAKTPEWA APICGVEAHV IRDLAKTLVK GRTQFMMGWC 

       370        380        390        400        410        420 
IQRQQHGEQP YWMAAVLATM IGQIGLPGGG ISYGHHYSSI GVPSSGAAAP GAFPRNLDEN 

       430        440        450        460        470        480 
QKPLFDSSDF KGASSTIPVA RWIDAILEPG KTIDANGSKV VYPDIKMMIF SGNNPWNHHQ 

       490        500        510        520        530        540 
DRNRMKQAFH KLECVVTVDV NWTATCRFSD IVLPACTTYE RNDIDVYGAY ANRGILAMQK 

       550        560        570        580        590        600 
MVEPLFDSLS DFEIFTRFAA VLGKEKEYTR NMGEMEWLET LYNECKAANA GKFEMPDFAT 

       610        620        630        640        650        660 
FWKQGYVHFG DGEVWTRHAD FRNDPEINPL GTPSGLIEIF SRKIDQFGYD DCKGHPTWME 

       670        680        690        700        710        720 
KTERSHGGPG SDKHPIWLQS CHPDKRLHSQ MCESREYRET YAVNGREPVY ISPVDAKARG 

       730        740        750        760        770        780 
IKDGDIVRVF NDRGQLLAGA VVSDNFPKGI VRIHEGAWYG PVGKDGSTEG GAEVGALCSY 

       790        800        810        820 
GDPNTLTLDI GTSKLAQACS AYTCLVEFEK YQGKVPKVSS FDGPIEVEI

« Hide

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References

[1]"Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species."
Dos Santos J.P., Iobbi-Nivol C., Couillault C., Giordano G., Mejean V.
J. Mol. Biol. 284:421-433(1998) [PubMed: 9813127] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-61, INDUCTION.
[2]"Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5-A resolution."
Czjzek M., Dos Santos J.P., Pommier J., Giordano G., Mejean V., Haser R.
J. Mol. Biol. 284:435-447(1998) [PubMed: 9813128] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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Cross-references

Sequence databases

AJ006085 Genomic DNA. Translation: CAA06851.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TMOX-ray2.50A1-829[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.6.6.9. 257419.
1.7.2.3. 257419.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_fold.
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]
TIGRFAMsTIGR01409. 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...

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Entry information

Entry nameTORA_SHEMA
AccessionPrimary (citable) accession number: O87948
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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