[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 43-59. STRAIN=DSM 938 / 37b4; DOI=10.1016/0005-2728(96)00092-8; PubMed=8856102 [NCBI, ExPASy, EBI, Israel, Japan] Shaw A.L., Hanson G.R., McEwan A.G.; "Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus."; Biochim. Biophys. Acta 1276:176-180(1996).
[2]	SEQUENCE REVISION. Shaw A.L., McEwan A.G.; Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 938 / 37b4; DOI=10.1006/jmbi.1996.0554; PubMed=8890911 [NCBI, ExPASy, EBI, Israel, Japan] Knaeblein J., Mann K., Ehlert S., Fonstein M., Huber R., Schneider F.; "Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus."; J. Mol. Biol. 263:40-52(1996).
[4]	X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS). STRAIN=DSM 938 / 37b4; DOI=10.1006/jmbi.1996.0555; PubMed=8890912 [NCBI, ExPASy, EBI, Israel, Japan] Schneider F., Loewe J., Huber R., Schindelin H., Kisker C., Knaeblein J.; "Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88-A resolution."; J. Mol. Biol. 263:53-69(1996).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). STRAIN=H123; McAlpine A.S., McEwan A.G., Shaw A.L., Bailey S.; "Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-A resolution and the dithionite-reduced enzyme at 2.8-A resolution."; J. Biol. Inorg. Chem. 2:690-700(1997).
[6]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). STRAIN=H123; DOI=10.1006/jmbi.2000.3702; PubMed=10835270 [NCBI, ExPASy, EBI, Israel, Japan] Stewart L.J., Bailey S., Bennett B., Charnock J.M., Garner C.D., McAlpine A.S.; "Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site."; J. Mol. Biol. 299:593-600(2000).
[7]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). STRAIN=H123; DOI=10.1021/bi0000521; PubMed=10985771 [NCBI, ExPASy, EBI, Israel, Japan] Bray R.C., Adams B., Smith A.T., Bennett B., Bailey S.; "Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family."; Biochemistry 39:11258-11269(2000).

Comments

FUNCTION: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds.
CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit + H₂O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H⁺.
COFACTOR: Binds 1 molybdenum ion per subunit.
COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Periplasm.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
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

U49506; AAD13674.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X95407; CAA64689.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1DMR; X-ray; 1.82 A; A=1-823.	[ExPASy / RCSB / EBI]
1DMS; X-ray; 1.88 A; A=43-823.	[ExPASy / RCSB / EBI]
1E18; X-ray; 2.00 A; A=1-823.	[ExPASy / RCSB / EBI]
1E5V; X-ray; 2.40 A; A/C=1-823.	[ExPASy / RCSB / EBI]
1E60; X-ray; 2.00 A; A/C=1-823.	[ExPASy / RCSB / EBI]
1E61; X-ray; 1.90 A; A/C=1-823.	[ExPASy / RCSB / EBI]
1H5N; X-ray; 2.00 A; A/C=1-823.	[ExPASy / RCSB / EBI]
2DMR; X-ray; 2.80 A; A=1-823.	[ExPASy / RCSB / EBI]
3DMR; X-ray; 2.50 A; A=1-823.	[ExPASy / RCSB / EBI]
4DMR; X-ray; 1.90 A; A=1-823.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DMR; -.
1DMS; -.
1E18; -.
1E5V; -.
1E60; -.
1E61; -.
1H5N; -.
2DMR; -.
3DMR; -.
4DMR; -.

ModBase

Q52675.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
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.
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.

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).

Other

DB01093; Dimethyl sulfoxide.

LinkHub

Q52675; -.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 42`	`42`	`Tat-type signal.`
`CHAIN`	`43 823`	`781`	`Dimethyl sulfoxide/trimethylamine N-oxide reductase.`	`PRO_0000019145`
`ACT_SITE`	`189 189`
`METAL`	`189 189`		`Molybdenum.`
`CONFLICT`	`33 33`		`R -> P (in Ref. 3; CAA64689).`
`CONFLICT`	`354 354`		`I -> K (in Ref. 3; CAA64689).`
`CONFLICT`	`410 410`		`T -> S (in Ref. 3; CAA64689).`
`CONFLICT`	`769 769`		`P -> A (in Ref. 3; CAA64689).`
`STRAND`	`48 54`	`7`
`STRAND`	`57 64`	`8`
`STRAND`	`67 73`	`7`
`HELIX`	`84 92`	`9`
`STRAND`	`101 103`	`3`
`HELIX`	`104 109`	`6`
`HELIX`	`110 112`	`3`
`HELIX`	`115 117`	`3`
`STRAND`	`123 125`	`3`
`HELIX`	`128 146`	`19`
`HELIX`	`148 150`	`3`
`HELIX`	`167 178`	`12`
`STRAND`	`182 186`	`5`
`STRAND`	`188 190`	`3`
`HELIX`	`193 200`	`8`
`STRAND`	`201 203`	`3`
`HELIX`	`213 219`	`7`
`STRAND`	`221 227`	`7`
`HELIX`	`230 233`	`4`
`STRAND`	`238 240`	`3`
`HELIX`	`245 255`	`11`
`STRAND`	`258 262`	`5`
`HELIX`	`268 273`	`6`
`STRAND`	`276 278`	`3`
`HELIX`	`285 298`	`14`
`HELIX`	`304 310`	`7`
`HELIX`	`314 321`	`8`
`TURN`	`322 326`	`5`
`HELIX`	`332 339`	`8`
`HELIX`	`343 355`	`13`
`STRAND`	`358 362`	`5`
`HELIX`	`365 367`	`3`
`TURN`	`370 372`	`3`
`HELIX`	`373 386`	`14`
`STRAND`	`395 398`	`4`
`TURN`	`403 406`	`4`
`HELIX`	`422 424`	`3`
`STRAND`	`432 434`	`3`
`STRAND`	`437 440`	`4`
`HELIX`	`441 443`	`3`
`HELIX`	`444 449`	`6`
`STRAND`	`454 457`	`4`
`STRAND`	`460 463`	`4`
`STRAND`	`469 474`	`6`
`HELIX`	`477 480`	`4`
`HELIX`	`484 490`	`7`
`HELIX`	`491 493`	`3`
`STRAND`	`495 503`	`9`
`HELIX`	`506 509`	`4`
`STRAND`	`512 517`	`6`
`HELIX`	`520 522`	`3`
`STRAND`	`525 529`	`5`
`TURN`	`531 533`	`3`
`STRAND`	`536 540`	`5`
`HELIX`	`553 563`	`11`
`HELIX`	`567 571`	`5`
`HELIX`	`576 593`	`18`
`HELIX`	`601 607`	`7`
`STRAND`	`609 611`	`3`
`HELIX`	`617 619`	`3`
`HELIX`	`624 628`	`5`
`TURN`	`630 632`	`3`
`STRAND`	`640 645`	`6`
`HELIX`	`647 652`	`6`
`STRAND`	`679 682`	`4`
`STRAND`	`687 690`	`4`
`TURN`	`694 696`	`3`
`HELIX`	`698 702`	`5`
`STRAND`	`710 713`	`4`
`HELIX`	`715 720`	`6`
`STRAND`	`728 732`	`5`
`STRAND`	`737 744`	`8`
`STRAND`	`752 754`	`3`
`STRAND`	`773 775`	`3`
`HELIX`	`778 780`	`3`
`TURN`	`789 791`	`3`
`STRAND`	`800 805`	`6`
`HELIX`	`820 822`	`3`

Sequence information

Length: 823 AA [This is the length of the unprocessed precursor]

Molecular weight: 89561 Da [This is the MW of the unprocessed precursor]

CRC64: 0E5E901CF2D69273 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKFSGNELR AELYRRAFLS YSVAPGALGM FGRSLLAKGA RAEALANGTV MSGSHWGVFT 

        70         80         90        100        110        120 
ATVENGRATA FTPWEKDPHP TPMLEGVLDS IYSPTRIKYP MVRREFLEKG VNADRSTRGN 

       130        140        150        160        170        180 
GDFVRVSWDQ ALDLVAAEVK RVEETYGPQG VFGGSYGWKS PGRLHNCTTL LRRMLTLAGG 

       190        200        210        220        230        240 
YVNGAGDYST GAAQVIMPHV VGTLEVYEQQ TAWPVLAENT EVMVFWAADP IKTSQIGWVI 

       250        260        270        280        290        300 
PEHGAYPGLE ALKAKGTKVI VIDPVRTKTV EFFGADHVTP KPQTDVAIML GMAHTLVAED 

       310        320        330        340        350        360 
LYDKDFIANY TSGFDKFLPY LMGETDSTPK TAEWASDISG VPAETIKELA RLFISKRTML 

       370        380        390        400        410        420 
AAGWSMQRMH HGEQAHWMLV TLASMLGQIG LPGGGFGLSY HYSGGGTPST SGPALSGITD 

       430        440        450        460        470        480 
GGAATKGPEW LAASGASVIP VARVVDMLEN PGAEFDFNGT RSKFPDVKMA YWVGGNPFVH 

       490        500        510        520        530        540 
HQDRNRMVKA WEKLETFIVH DFQWTPTARH ADIVLPATTS YERNDIETIG DYSNTGILAM 

       550        560        570        580        590        600 
KKIVEPLYEA RSDYDIFAAV AERLGKGKEF TEGKDEMGWI KSFYDDAAKQ GKAGGVEMPA 

       610        620        630        640        650        660 
FDAFWAEGIV EFPVTDGADF VRYASFREDP LLNPLGTPTG LIEIYSKNIE KMGYDDCPAH 

       670        680        690        700        710        720 
PTWMEPLERL DGPGAKYPLH IAASHPFNRL HSQLNGTVLR EGYAVQGHEP CLMHPDDAAA 

       730        740        750        760        770        780 
RGIADGDVVR VHNDRGQILT GVKVTDAVMK GVIQIYEGGW YDPSDVTEPG TLDKYGDVNV 

       790        800        810        820 
LSADIGTSKL AQGNCGQTVL AEVEKYTGPA VTLTGFVAPK AAE

Q52675 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