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Protein

Dimethyl sulfoxide/trimethylamine N-oxide reductase

Gene

dorA

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Mo-bis(molybdopterin guanine dinucleotide)2 PublicationsNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581Molybdopterin guanine dinucleotide 26 Publications
Metal bindingi189 – 1891Molybdenum
Binding sitei368 – 3681Molybdopterin guanine dinucleotide 16 Publications
Binding sitei476 – 4761Molybdopterin guanine dinucleotide 16 Publications
Binding sitei480 – 4801Molybdopterin guanine dinucleotide 16 Publications
Binding sitei523 – 5231Molybdopterin guanine dinucleotide 16 Publications
Binding sitei553 – 5531Molybdopterin guanine dinucleotide 16 Publications
Binding sitei779 – 7791Molybdopterin guanine dinucleotide 16 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAi1.8.5.3. 5381.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethyl sulfoxide/trimethylamine N-oxide reductase (EC:1.7.2.3, EC:1.8.5.3)
Short name:
DMSO reductase
Short name:
DMSOR
Short name:
Me2SO reductase
Short name:
TMAOR
Gene namesi
Name:dorA
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Tat-type signalPROSITE-ProRule annotation2 PublicationsAdd
BLAST
Chaini43 – 823781Dimethyl sulfoxide/trimethylamine N-oxide reductasePRO_0000019145Add
BLAST

Post-translational modificationi

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

Interactioni

Subunit structurei

Homodimer.8 Publications

Protein-protein interaction databases

STRINGi272942.RCAP_rcc02845.

Structurei

Secondary structure

1
823
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 547Combined sources
Beta strandi57 – 648Combined sources
Beta strandi67 – 737Combined sources
Helixi84 – 929Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 1096Combined sources
Helixi110 – 1123Combined sources
Helixi115 – 1173Combined sources
Beta strandi123 – 1253Combined sources
Helixi128 – 14619Combined sources
Helixi148 – 1503Combined sources
Helixi167 – 17812Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi188 – 1903Combined sources
Helixi193 – 2008Combined sources
Beta strandi201 – 2033Combined sources
Helixi213 – 2197Combined sources
Beta strandi221 – 2277Combined sources
Helixi230 – 2334Combined sources
Beta strandi238 – 2403Combined sources
Helixi245 – 25511Combined sources
Beta strandi258 – 2625Combined sources
Helixi268 – 2736Combined sources
Beta strandi276 – 2783Combined sources
Helixi285 – 29814Combined sources
Helixi304 – 3107Combined sources
Helixi314 – 3218Combined sources
Turni322 – 3265Combined sources
Helixi332 – 3398Combined sources
Helixi343 – 35513Combined sources
Beta strandi358 – 3625Combined sources
Helixi365 – 3673Combined sources
Turni370 – 3723Combined sources
Helixi373 – 38614Combined sources
Beta strandi395 – 3984Combined sources
Turni403 – 4064Combined sources
Helixi422 – 4243Combined sources
Helixi429 – 4313Combined sources
Beta strandi432 – 4343Combined sources
Beta strandi437 – 4404Combined sources
Helixi441 – 4433Combined sources
Helixi444 – 4496Combined sources
Beta strandi454 – 4574Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi469 – 4746Combined sources
Helixi477 – 4804Combined sources
Helixi484 – 4907Combined sources
Helixi491 – 4933Combined sources
Beta strandi495 – 5039Combined sources
Helixi506 – 5094Combined sources
Beta strandi512 – 5176Combined sources
Helixi520 – 5223Combined sources
Beta strandi525 – 5295Combined sources
Turni531 – 5333Combined sources
Beta strandi536 – 5405Combined sources
Helixi553 – 56311Combined sources
Helixi567 – 5715Combined sources
Helixi576 – 59318Combined sources
Helixi601 – 6077Combined sources
Beta strandi609 – 6113Combined sources
Helixi617 – 6193Combined sources
Helixi624 – 6285Combined sources
Turni630 – 6323Combined sources
Beta strandi640 – 6456Combined sources
Helixi647 – 6526Combined sources
Beta strandi679 – 6824Combined sources
Beta strandi687 – 6904Combined sources
Turni694 – 6963Combined sources
Helixi698 – 7025Combined sources
Beta strandi710 – 7134Combined sources
Helixi715 – 7206Combined sources
Beta strandi728 – 7325Combined sources
Beta strandi737 – 7448Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi773 – 7753Combined sources
Helixi778 – 7803Combined sources
Turni789 – 7913Combined sources
Beta strandi800 – 8056Combined sources
Beta strandi815 – 8173Combined sources
Helixi820 – 8223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ52675.
SMRiQ52675. Positions 45-823.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ52675.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 1605MGD 1 binding
Regioni232 – 2332MGD 2 binding
Regioni262 – 2632MGD 2 binding
Regioni283 – 2853MGD 2 binding
Regioni364 – 3652MGD 2 binding
Regioni500 – 5012MGD 1 binding
Regioni685 – 6862MGD 1 binding
Regioni691 – 6933MGD 1 binding
Regioni796 – 7972MGD 1 binding

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108J2R. Bacteria.
COG0243. LUCA.

Family and domain databases

InterProiIPR009010. 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]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR00509. bisC_fam. 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.

Q52675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKFSGNELR AELYRRAFLS YSVAPGALGM FGRSLLAKGA RAEALANGTV
60 70 80 90 100
MSGSHWGVFT ATVENGRATA FTPWEKDPHP TPMLEGVLDS IYSPTRIKYP
110 120 130 140 150
MVRREFLEKG VNADRSTRGN GDFVRVSWDQ ALDLVAAEVK RVEETYGPQG
160 170 180 190 200
VFGGSYGWKS PGRLHNCTTL LRRMLTLAGG YVNGAGDYST GAAQVIMPHV
210 220 230 240 250
VGTLEVYEQQ TAWPVLAENT EVMVFWAADP IKTSQIGWVI PEHGAYPGLE
260 270 280 290 300
ALKAKGTKVI VIDPVRTKTV EFFGADHVTP KPQTDVAIML GMAHTLVAED
310 320 330 340 350
LYDKDFIANY TSGFDKFLPY LMGETDSTPK TAEWASDISG VPAETIKELA
360 370 380 390 400
RLFISKRTML AAGWSMQRMH HGEQAHWMLV TLASMLGQIG LPGGGFGLSY
410 420 430 440 450
HYSGGGTPST SGPALSGITD GGAATKGPEW LAASGASVIP VARVVDMLEN
460 470 480 490 500
PGAEFDFNGT RSKFPDVKMA YWVGGNPFVH HQDRNRMVKA WEKLETFIVH
510 520 530 540 550
DFQWTPTARH ADIVLPATTS YERNDIETIG DYSNTGILAM KKIVEPLYEA
560 570 580 590 600
RSDYDIFAAV AERLGKGKEF TEGKDEMGWI KSFYDDAAKQ GKAGGVEMPA
610 620 630 640 650
FDAFWAEGIV EFPVTDGADF VRYASFREDP LLNPLGTPTG LIEIYSKNIE
660 670 680 690 700
KMGYDDCPAH PTWMEPLERL DGPGAKYPLH IAASHPFNRL HSQLNGTVLR
710 720 730 740 750
EGYAVQGHEP CLMHPDDAAA RGIADGDVVR VHNDRGQILT GVKVTDAVMK
760 770 780 790 800
GVIQIYEGGW YDPSDVTEPG TLDKYGDVNV LSADIGTSKL AQGNCGQTVL
810 820
AEVEKYTGPA VTLTGFVAPK AAE
Length:823
Mass (Da):89,561
Last modified:July 15, 1999 - v2
Checksum:i0E5E901CF2D69273
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331R → P in CAA64689 (PubMed:8890911).Curated
Sequence conflicti354 – 3541I → K in CAA64689 (PubMed:8890911).Curated
Sequence conflicti410 – 4101T → S in CAA64689 (PubMed:8890911).Curated
Sequence conflicti769 – 7691P → A in CAA64689 (PubMed:8890911).Curated

Mass spectrometryi

Molecular mass is 86600 Da from positions 43 - 823. Determined by MALDI. 1 Publication
Molecular mass is 85034 Da from positions 43 - 823. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49506 Genomic DNA. Translation: AAD13674.1.
X95407 Genomic DNA. Translation: CAA64689.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49506 Genomic DNA. Translation: AAD13674.1.
X95407 Genomic DNA. Translation: CAA64689.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ52675.
SMRiQ52675. Positions 45-823.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc02845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108J2R. Bacteria.
COG0243. LUCA.

Enzyme and pathway databases

BRENDAi1.8.5.3. 5381.

Miscellaneous databases

EvolutionaryTraceiQ52675.

Family and domain databases

InterProiIPR009010. 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]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR00509. bisC_fam. 1 hit.
PROSITEiPS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiDSTOR_RHOCA
AccessioniPrimary (citable) accession number: Q52675
Secondary accession number(s): P72249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1999
Last modified: November 11, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.