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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)DescriptionActionsGraphical viewLength
Metal bindingi180Molybdenum1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST31
ChainiPRO_000001915732 – 829Trimethylamine-N-oxide reductaseAdd BLAST798

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

1829
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 45Combined sources5
Beta strandi48 – 55Combined sources8
Beta strandi58 – 64Combined sources7
Helixi73 – 76Combined sources4
Helixi78 – 82Combined sources5
Beta strandi92 – 94Combined sources3
Helixi95 – 100Combined sources6
Helixi101 – 103Combined sources3
Helixi106 – 108Combined sources3
Beta strandi113 – 116Combined sources4
Helixi119 – 136Combined sources18
Helixi139 – 141Combined sources3
Turni154 – 156Combined sources3
Helixi158 – 167Combined sources10
Beta strandi173 – 176Combined sources4
Beta strandi179 – 181Combined sources3
Helixi184 – 191Combined sources8
Helixi204 – 210Combined sources7
Beta strandi212 – 218Combined sources7
Helixi221 – 224Combined sources4
Beta strandi229 – 231Combined sources3
Helixi236 – 248Combined sources13
Beta strandi251 – 257Combined sources7
Helixi263 – 268Combined sources6
Beta strandi271 – 273Combined sources3
Helixi280 – 293Combined sources14
Helixi299 – 305Combined sources7
Helixi309 – 317Combined sources9
Turni318 – 321Combined sources4
Helixi327 – 334Combined sources8
Helixi338 – 350Combined sources13
Beta strandi353 – 357Combined sources5
Helixi360 – 362Combined sources3
Turni365 – 367Combined sources3
Helixi368 – 381Combined sources14
Beta strandi390 – 393Combined sources4
Turni398 – 401Combined sources4
Beta strandi435 – 438Combined sources4
Helixi439 – 441Combined sources3
Helixi442 – 447Combined sources6
Beta strandi452 – 454Combined sources3
Beta strandi456 – 461Combined sources6
Beta strandi467 – 472Combined sources6
Helixi475 – 478Combined sources4
Helixi482 – 489Combined sources8
Beta strandi493 – 501Combined sources9
Helixi504 – 507Combined sources4
Beta strandi510 – 515Combined sources6
Helixi518 – 520Combined sources3
Beta strandi523 – 527Combined sources5
Turni529 – 531Combined sources3
Beta strandi534 – 538Combined sources5
Helixi551 – 561Combined sources11
Helixi565 – 569Combined sources5
Helixi574 – 589Combined sources16
Turni590 – 592Combined sources3
Helixi598 – 604Combined sources7
Beta strandi606 – 608Combined sources3
Helixi619 – 623Combined sources5
Turni625 – 627Combined sources3
Beta strandi631 – 640Combined sources10
Helixi642 – 645Combined sources4
Beta strandi665 – 668Combined sources4
Turni669 – 673Combined sources5
Beta strandi676 – 679Combined sources4
Beta strandi684 – 687Combined sources4
Turni691 – 693Combined sources3
Helixi695 – 698Combined sources4
Turni699 – 701Combined sources3
Beta strandi708 – 711Combined sources4
Helixi713 – 718Combined sources6
Beta strandi726 – 730Combined sources5
Beta strandi735 – 742Combined sources8
Beta strandi750 – 752Combined sources3
Helixi769 – 772Combined sources4
Beta strandi777 – 780Combined sources4
Helixi783 – 785Combined sources3
Turni794 – 796Combined sources3
Beta strandi805 – 810Combined sources6
Beta strandi820 – 822Combined sources3

3D structure databases

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

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: November 2, 2016
This is version 90 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.