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Protein

Trimethylamine-N-oxide reductase

Gene

torA

Organism
Shewanella massilia
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+.

Cofactori

Mo-bis(molybdopterin guanine dinucleotide)1 PublicationNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi180 – 1801Molybdenum

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAi1.7.2.3. 5705.

Names & Taxonomyi

Protein namesi
Recommended name:
Trimethylamine-N-oxide reductase (EC:1.7.2.3)
Short name:
TMAO reductase
Short name:
Trimethylamine oxidase
Gene namesi
Name:torA
OrganismiShewanella massilia
Taxonomic identifieri76854 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Tat-type signalPROSITE-ProRule annotation1 PublicationAdd
BLAST
Chaini32 – 829798Trimethylamine-N-oxide reductasePRO_0000019157Add
BLAST

Post-translational modificationi

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

Expressioni

Inductioni

By TMAO and DMSO.1 Publication

Structurei

Secondary structure

1
829
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 455Combined sources
Beta strandi48 – 558Combined sources
Beta strandi58 – 647Combined sources
Helixi73 – 764Combined sources
Helixi78 – 825Combined sources
Beta strandi92 – 943Combined sources
Helixi95 – 1006Combined sources
Helixi101 – 1033Combined sources
Helixi106 – 1083Combined sources
Beta strandi113 – 1164Combined sources
Helixi119 – 13618Combined sources
Helixi139 – 1413Combined sources
Turni154 – 1563Combined sources
Helixi158 – 16710Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi179 – 1813Combined sources
Helixi184 – 1918Combined sources
Helixi204 – 2107Combined sources
Beta strandi212 – 2187Combined sources
Helixi221 – 2244Combined sources
Beta strandi229 – 2313Combined sources
Helixi236 – 24813Combined sources
Beta strandi251 – 2577Combined sources
Helixi263 – 2686Combined sources
Beta strandi271 – 2733Combined sources
Helixi280 – 29314Combined sources
Helixi299 – 3057Combined sources
Helixi309 – 3179Combined sources
Turni318 – 3214Combined sources
Helixi327 – 3348Combined sources
Helixi338 – 35013Combined sources
Beta strandi353 – 3575Combined sources
Helixi360 – 3623Combined sources
Turni365 – 3673Combined sources
Helixi368 – 38114Combined sources
Beta strandi390 – 3934Combined sources
Turni398 – 4014Combined sources
Beta strandi435 – 4384Combined sources
Helixi439 – 4413Combined sources
Helixi442 – 4476Combined sources
Beta strandi452 – 4543Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi467 – 4726Combined sources
Helixi475 – 4784Combined sources
Helixi482 – 4898Combined sources
Beta strandi493 – 5019Combined sources
Helixi504 – 5074Combined sources
Beta strandi510 – 5156Combined sources
Helixi518 – 5203Combined sources
Beta strandi523 – 5275Combined sources
Turni529 – 5313Combined sources
Beta strandi534 – 5385Combined sources
Helixi551 – 56111Combined sources
Helixi565 – 5695Combined sources
Helixi574 – 58916Combined sources
Turni590 – 5923Combined sources
Helixi598 – 6047Combined sources
Beta strandi606 – 6083Combined sources
Helixi619 – 6235Combined sources
Turni625 – 6273Combined sources
Beta strandi631 – 64010Combined sources
Helixi642 – 6454Combined sources
Beta strandi665 – 6684Combined sources
Turni669 – 6735Combined sources
Beta strandi676 – 6794Combined sources
Beta strandi684 – 6874Combined sources
Turni691 – 6933Combined sources
Helixi695 – 6984Combined sources
Turni699 – 7013Combined sources
Beta strandi708 – 7114Combined sources
Helixi713 – 7186Combined sources
Beta strandi726 – 7305Combined sources
Beta strandi735 – 7428Combined sources
Beta strandi750 – 7523Combined sources
Helixi769 – 7724Combined sources
Beta strandi777 – 7804Combined sources
Helixi783 – 7853Combined sources
Turni794 – 7963Combined sources
Beta strandi805 – 8106Combined sources
Beta strandi820 – 8223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMOX-ray2.50A1-829[»]
ProteinModelPortaliO87948.
SMRiO87948. Positions 36-829.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO87948.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK07811.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006311. TAT_signal.
IPR011887. TorA.
[Graphical view]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR02164. torA. 1 hit.
PROSITEiPS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O87948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRRDFLKGI ASSSFVVLGG SSVLTPLNAL AKAGINEDEW LTTGSHFGAF
60 70 80 90 100
KMKRKNGVIA EVKPFDLDKY PTDMINGIRG MVYNPSRVRY PMVRLDFLLK
110 120 130 140 150
GHKSNTHQRG DFRFVRVTWD KALTLFKHSL DEVQTQYGPS GLHAGQTGWR
160 170 180 190 200
ATGQLHSSTS HMQRAVGMHG NYVKKIGDYS TGAGQTILPY VLGSTEVYAQ
210 220 230 240 250
GTSWPLILEH SDTIVLWSND PYKNLQVGWN AETHESFAYL AQLKEKVKQG
260 270 280 290 300
KIRVISIDPV VTKTQAYLGC EQLYVNPQTD VTLMLAIAHE MISKKLYDDK
310 320 330 340 350
FIQGYSLGFE EFVPYVMGTK DGVAKTPEWA APICGVEAHV IRDLAKTLVK
360 370 380 390 400
GRTQFMMGWC IQRQQHGEQP YWMAAVLATM IGQIGLPGGG ISYGHHYSSI
410 420 430 440 450
GVPSSGAAAP GAFPRNLDEN QKPLFDSSDF KGASSTIPVA RWIDAILEPG
460 470 480 490 500
KTIDANGSKV VYPDIKMMIF SGNNPWNHHQ DRNRMKQAFH KLECVVTVDV
510 520 530 540 550
NWTATCRFSD IVLPACTTYE RNDIDVYGAY ANRGILAMQK MVEPLFDSLS
560 570 580 590 600
DFEIFTRFAA VLGKEKEYTR NMGEMEWLET LYNECKAANA GKFEMPDFAT
610 620 630 640 650
FWKQGYVHFG DGEVWTRHAD FRNDPEINPL GTPSGLIEIF SRKIDQFGYD
660 670 680 690 700
DCKGHPTWME KTERSHGGPG SDKHPIWLQS CHPDKRLHSQ MCESREYRET
710 720 730 740 750
YAVNGREPVY ISPVDAKARG IKDGDIVRVF NDRGQLLAGA VVSDNFPKGI
760 770 780 790 800
VRIHEGAWYG PVGKDGSTEG GAEVGALCSY GDPNTLTLDI GTSKLAQACS
810 820
AYTCLVEFEK YQGKVPKVSS FDGPIEVEI
Length:829
Mass (Da):92,362
Last modified:November 1, 1998 - v1
Checksum:i6F58A59E8C41CF1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006085 Genomic DNA. Translation: CAA06851.1.

Genome annotation databases

KEGGiag:CAA06851.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006085 Genomic DNA. Translation: CAA06851.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMOX-ray2.50A1-829[»]
ProteinModelPortaliO87948.
SMRiO87948. Positions 36-829.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA06851.

Phylogenomic databases

KOiK07811.

Enzyme and pathway databases

BRENDAi1.7.2.3. 5705.

Miscellaneous databases

EvolutionaryTraceiO87948.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006311. TAT_signal.
IPR011887. TorA.
[Graphical view]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR02164. torA. 1 hit.
PROSITEiPS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH OXIDIZED MO-BIS-MGD, COFACTOR.

Entry informationi

Entry nameiTORA_SHEMA
AccessioniPrimary (citable) accession number: O87948
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.