FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions (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.
SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
CAUTION: Was originally (PubMed:7542800) assigned to be a biotin sulfoxide reductase hence the original gene designation of bisC.

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

L42023; AAC22303.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H64083; H64083.

RefSeq

NP_438803.1; -.

3D structure databases

HSSP

Q57366; 1EU1. [HSSP ENTRY / PDB]

ModBase

P44798.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0643-MON; -.

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

PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
PS00490; MOLYBDOPTERIN_PROK_2; 1.
PS00932; MOLYBDOPTERIN_PROK_3; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P44798.

Genome annotation databases

950790; -.

L42023_GR; HI0643.

hin:HI0643; -.

fig|71421.1.peg.613; -.

TIGR

HI0643; -.

Phylogenomic databases

HOGENOM

P44798; -.

Other

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 40`	`40`	`Tat-type signal (Potential).`
`CHAIN`	`41 825`	`785`	`Trimethylamine-N-oxide reductase.`	`PRO_0000019166`

Sequence information

Length: 825 AA [This is the length of the unprocessed precursor]

Molecular weight: 91053 Da [This is the MW of the unprocessed precursor]

CRC64: 4254287D42B45E5B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKNNVNEQR RDFLKKTSLG VAGSALSGGM VGVVSKSAVA KEAEMKTVVT AAHWGSIGVV 

        70         80         90        100        110        120 
VQDGKVVKSG PAIEPAVPNE LQTVVADQLY SERRVKCPMV RKGFLANPGK SDTTMRGRDE 

       130        140        150        160        170        180 
WVRVSWDEAL DLVHNQLKRV RDEHGSTGIF AGSYGWFSCG SLHASRTLLQ RYMNATGGFV 

       190        200        210        220        230        240 
GHKGDYSTGA AQVIMPHVLG TIEVYEQQTS WESILESSDI IVLWSANPLT TMRIAWMSTD 

       250        260        270        280        290        300 
QKGIEYFKKF QASGKRIICI DPQKSETCQM LNAEWIPVNT ATDVPLMLGI AHTLVEQGKH 

       310        320        330        340        350        360 
DKDFLKKYTS GYAKFEEYLL GKTDGQPKTA EWAAKICGVP AETIKQLAAD FASKRTMLMG 

       370        380        390        400        410        420 
GWGMQRQRHG EQTHWMLVTL ASMLGQIGLP GGGFGLSYHY SNGGVPTATG GIIGSITASP 

       430        440        450        460        470        480 
SGKAGAKTWL DDTSKSAFPL ARIADVLLHP GKKIQYNGTE ITYPDIKAVY WAGGNPFVHH 

       490        500        510        520        530        540 
QDTNTLVKAF QKPDVVIVNE VNWTPTARMA DIVLPATTSY ERNDLTMAGD YSMMSVYPMK 

       550        560        570        580        590        600 
QVVPPQFEAK NDYDIFVELA KRAGVEEQYT EGKTEMEWLE EFYNAAFSAA RANRVAMPRF 

       610        620        630        640        650        660 
DKFWAENKPL SFEAGEAAKK WVRYGEFRED PLLNPLGTPS GKIEIFSDVV EKMNYNDCKG 

       670        680        690        700        710        720 
HPSWMEPEEF AGNVTEEYPL ALVTPHPYYR LHSQLAHTSL RQKYAVNDRE PVMIHPEDAA 

       730        740        750        760        770        780 
ARGIKDGDIV RIHSKRGQVL AGAAVTENII KGTVALHEGA WYDPMYLGES EKPLCKNGCA 

       790        800        810        820 
NVLTRDEGTS KLAQGNSPNT CIVQIEKFIG VAPEVTVFKQ PKQVA

P44798 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