FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N-oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency (By similarity).
CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit + H₂O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H⁺.
COFACTOR: Molybdenum (molybdopterin) (By similarity).
SUBCELLULAR LOCATION: Periplasm (By similarity).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
MISCELLANEOUS: Expression of torYZ allows E.coli to grow anaerobically on a wider range of substrates than does expression of torCAD (By similarity).
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE014075; AAN80743.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_754178.1; -.

3D structure databases

HSSP

Q52675; 1E61. [HSSP ENTRY / PDB]

ModBase

Q8CVZ3.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0050626;	Molecular function: trimethylamine-N-oxide reductase (cytochrome c) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR009010; Asp_de-COase-like_fold.
IPR006658; BisC.
IPR006656; Mopterin_OxRdtase.
IPR006655; Mopterin_OxRdtase_prok_CS.
IPR006657; MPT_dinuc_bd.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.

Pfam

PF00384; Molybdopterin; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00509; bisC_fam; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS00490; MOLYBDOPTERIN_PROK_2; 1.
PS00932; MOLYBDOPTERIN_PROK_3; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

1036854; -.

AE014075_GR; c2286.

ecc:c2286; -.

fig|199310.1.peg.2221; -.

Phylogenomic databases

HOGENOM

Q8CVZ3; -.

Genome annotation databases

CMR

Q8CVZ3; c2286.

Other

ProtoNet

Q8CVZ3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Molybdenum; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`	`Tat-type signal (Potential).`
`CHAIN`	`32 809`	`778`	`Trimethylamine-N-oxide reductase 2.`	`PRO_0000019164`

Sequence information

Length: 809 AA [This is the length of the unprocessed precursor]

Molecular weight: 89006 Da [This is the MW of the unprocessed precursor]

CRC64: 07087EB335CDEF22 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTLTRREFIK HSGIAAGTLV VTSAAPLPAW AEEKGGKILT AGRWGAMNVE VKDGKIVSST 

        70         80         90        100        110        120 
GALAKTIPNS LQSTAADQVH TTARIQHPMV RKSYLDNPLQ PVKGRGEDTY VQVSWEQALK 

       130        140        150        160        170        180 
LIHEQHDRIR KANGPSAIFA GSYGWRSSGV LHKAQTLLQR YMNLAGGYSG HSGDYSTGAA 

       190        200        210        220        230        240 
QVIMPHVVGS VEVYEQQTSW PLILENSQVV VLWGMNPLNT LKIAWSSTDE QGLEYFHQLK 

       250        260        270        280        290        300 
KSGKPVIAID PIRSETIEFF GDNATWIAPN MGTDVALMLG IAHTLMTQGK HDKVFLEKYT 

       310        320        330        340        350        360 
TGYPQFEEYL TGKSDNTPKS AAWAAEITGV PEAQIVKLAE LMAANRTMLM AGWGIQRQQY 

       370        380        390        400        410        420 
GEQKHWMLVT LAAMLGQIGT PGGGFGFSYH YSNGGNPTRV GGVLPEMSAA IAGQASEAAD 

       430        440        450        460        470        480 
DGGMTAIPVA RIVDALENPG GKYQHNGKEQ TYPNIKMIWW AGGGNFTHHQ DTNRLIKAWQ 

       490        500        510        520        530        540 
KPEMIVVSEC YWTAAAKHAD IVLPITTSFE RNDLTMTGDY SNQHIVLMKQ AVAPQFEARN 

       550        560        570        580        590        600 
DFDVFADLAE LLKPGGKEIY TEGKDEMAWL KFFYDAAQKG ARAQRVTMPM FNAFWQQNKL 

       610        620        630        640        650        660 
IEMRRSEKNE QYIRYGDFRA DPVKNALGTP SGKIEIYSRT LEKFGYKDCP AHPTWLAPDE 

       670        680        690        700        710        720 
WKGTADEKQL QLLTAHPAHR LHSQLNYAEL RKKYAVADRE PITIHTEDAA RFGIANGDLV 

       730        740        750        760        770        780 
RVWNKRGQIL TGAVVTDGIK KGVVCVHEGA WPDLENGLCK NGSANVLTAD IPSSQLANAC 

       790        800 
AGNSALVYIE KYTGNALKLT AFDQPAVQA

Q8CVZ3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools