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Q52675 (DSTOR_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dimethyl sulfoxide/trimethylamine N-oxide reductase
Short name=DMSO reductase
Short name=DMSOR
Short name=Me2SO reductase
Short name=TMAOR
EC=1.7.2.3
EC=1.8.5.3
Gene names
Name:dorA
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of dimethyl sulfoxide (DMSO) and trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and trimethylamine, respectively. The terminal DMSO reductase can also use various sulfoxides and N-oxide compounds as terminal electron acceptor in addition to DMSO and TMAO. Ref.1 Ref.4

Catalytic activity

Dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol.

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

Cofactor

Binds 1 molybdenum ion per subunit. Ref.4 Ref.5

Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit. Ref.4 Ref.5

Subunit structure

Homodimer. Ref.1 Ref.4 Ref.8 Ref.10

Subcellular location

Periplasm Ref.1.

Post-translational modification

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

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Mass spectrometry

Molecular mass is 86600 Da from positions 43 - 823. Determined by MALDI. Ref.3

Molecular mass is 85034 Da from positions 43 - 823. Determined by ESI. Ref.3

Sequence caution

The sequence CAA64689.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Molybdenum
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

molybdenum ion binding

Inferred from electronic annotation. Source: InterPro

trimethylamine-N-oxide reductase (cytochrome c) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242Tat-type signal Ref.1 Ref.3
Chain43 – 823781Dimethyl sulfoxide/trimethylamine N-oxide reductase
PRO_0000019145

Regions

Region156 – 1605Molybdopterin 1 binding
Region232 – 2332Molybdopterin 2 binding
Region262 – 2632Molybdopterin 2 binding
Region283 – 2853Molybdopterin 2 binding
Region364 – 3652Molybdopterin 2 binding
Region500 – 5012Molybdopterin 1 binding
Region685 – 6862Molybdopterin 1 binding
Region691 – 6933Molybdopterin 1 binding
Region796 – 7972Molybdopterin 1 binding

Sites

Active site1891
Metal binding1561Molybdenum
Binding site1581Molybdopterin 2
Binding site1891Molybdopterin 1
Binding site1891Molybdopterin 2
Binding site3681Molybdopterin 1
Binding site4761Molybdopterin 1
Binding site4801Molybdopterin 1
Binding site5231Molybdopterin 1
Binding site5531Molybdopterin 1
Binding site7791Molybdopterin 1

Experimental info

Sequence conflict331R → P in CAA64689. Ref.3
Sequence conflict3541I → K in CAA64689. Ref.3
Sequence conflict4101T → S in CAA64689. Ref.3
Sequence conflict7691P → A in CAA64689. Ref.3

Secondary structure

1 ........................................................................................................................................................ 823
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q52675 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 0E5E901CF2D69273

FASTA82389,561
        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

« Hide

References

[1]"Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus."
Shaw A.L., Hanson G.R., McEwan A.G.
Biochim. Biophys. Acta 1276:176-180(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-59, FUNCTION AS A DIMETHYL SULFOXIDE REDUCTASE AND TRIMETHYLAMINE N-OXIDE REDUCTASE, SUBCELLULAR LOCATION, SUBUNIT.
Strain: DSM 938 / 37b4.
[2]Shaw A.L., McEwan A.G.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus."
Knaeblein J., Mann K., Ehlert S., Fonstein M., Huber R., Schneider F.
J. Mol. Biol. 263:40-52(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-71, MASS SPECTROMETRY.
Strain: DSM 938 / 37b4.
[4]"Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme."
McEwan A.G., Ferguson S.J., Jackson J.B.
Biochem. J. 274:305-307(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A DIMETHYL SULFOXIDE REDUCTASE AND TRIMETHYLAMINE N-OXIDE REDUCTASE, COFACTOR, SUBUNIT.
Strain: DSM 938 / 37b4.
[5]"Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88-A resolution."
Schneider F., Loewe J., Huber R., Schindelin H., Kisker C., Knaeblein J.
J. Mol. Biol. 263:53-69(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 43-823 IN COMPLEX WITH MOLYBDOPTERIN, COFACTOR.
[6]"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."
McAlpine A.S., McEwan A.G., Shaw A.L., Bailey S.
J. Biol. Inorg. Chem. 2:690-700(1997)
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN.
Strain: H123.
[7]"The high resolution crystal structure of DMSO reductase in complex with DMSO."
McAlpine A.S., McEwan A.G., Bailey S.
J. Mol. Biol. 275:613-623(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN.
[8]"Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family."
Bray R.C., Adams B., Smith A.T., Bennett B., Bailey S.
Biochemistry 39:11258-11269(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN, SUBUNIT.
[9]"Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site."
Stewart L.J., Bailey S., Bennett B., Charnock J.M., Garner C.D., McAlpine A.S.
J. Mol. Biol. 299:593-600(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN.
[10]"Reactions of dimethylsulfoxide reductase in the presence of dimethyl sulfide and the structure of the dimethyl sulfide-modified enzyme."
Bray R.C., Adams B., Smith A.T., Richards R.L., Lowe D.J., Bailey S.
Biochemistry 40:9810-9820(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U49506 Genomic DNA. Translation: AAD13674.1.
X95407 Genomic DNA. Translation: CAA64689.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMRX-ray1.82A1-823[»]
1DMSX-ray1.88A43-823[»]
1E18X-ray2.00A1-823[»]
1E5VX-ray2.40A/C1-823[»]
1E60X-ray2.00A/C1-823[»]
1E61X-ray1.90A/C1-823[»]
1H5NX-ray2.00A/C1-823[»]
2DMRX-ray2.80A1-823[»]
3DMRX-ray2.50A1-823[»]
4DMRX-ray1.90A1-823[»]
ProteinModelPortalQ52675.
SMRQ52675. Positions 45-823.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.40.20. 1 hit.
InterProIPR009010. Asp_de-COase-like_dom.
IPR006658. BisC.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR00509. bisC_fam. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. False negative.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01093. Dimethyl sulfoxide.
EvolutionaryTraceQ52675.

Entry information

Entry nameDSTOR_RHOCA
AccessionPrimary (citable) accession number: Q52675
Secondary accession number(s): P72249
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1999
Last modified: May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents