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Q57366 (DSTOR_RHOSH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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:dmsA
Synonyms:dsrA
OrganismRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifier1063 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length822 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.6

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 Ref.7 Ref.8

Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit. Ref.4 Ref.5 Ref.7 Ref.8

Subunit structure

Homodimer. Ref.8

Subcellular location

Periplasm Ref.5.

Post-translational modification

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

Disruption phenotype

Disruption of dmsA results in the inability to use DMSO or TMAO as the terminal electron acceptor in anaerobic respiration and in greatly diminished in vitro DMSOR activity. Ref.6

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

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.2 Ref.3
Chain43 – 822780Dimethyl sulfoxide/trimethylamine N-oxide reductase
PRO_0000019146

Regions

Region158 – 1603Molybdopterin 1 binding
Region232 – 2332Molybdopterin 2 binding
Region262 – 2632Molybdopterin 2 binding
Region283 – 2853Molybdopterin 2 binding
Region364 – 3652Molybdopterin 2 binding
Region500 – 5012Molybdopterin 1 binding
Region683 – 6864Molybdopterin 1 binding
Region691 – 6933Molybdopterin 1 binding
Region796 – 7972Molybdopterin 1 binding

Sites

Active site1891
Active site1891 By similarity
Metal binding1561Molybdenum By similarity
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 site6891Molybdopterin 1
Binding site7791Molybdopterin 1

Experimental info

Sequence conflict1851S → V in AAC13660. Ref.3
Sequence conflict1921A → G in AAC13660. Ref.3
Sequence conflict1991H → Y in AAC13660. Ref.3
Sequence conflict371 – 3733HGE → MAQ in AAC13660. Ref.3
Sequence conflict4221G → A in AAC13660. Ref.3
Sequence conflict4301W → C in AAC13660. Ref.3
Sequence conflict6951N → T in AAC13660. Ref.3
Sequence conflict7061A → V in AAC13660. Ref.3
Sequence conflict7421A → T in AAC13660. Ref.3
Sequence conflict7491M → I in AAC13660. Ref.3
Sequence conflict7931G → D in AAC13660. Ref.3

Secondary structure

1 ................................................................................................................................................ 822
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q57366 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4AB3497E5D26B1C9

FASTA82289,208
        10         20         30         40         50         60 
MTKLSGQELH AELSRRAFLS YTAAVGALGL CGTSLLAQGA RAEGLANGEV MSGCHWGVFK 

        70         80         90        100        110        120 
ARVENGRAVA FEPWDKDPAP SHQLPGVLDS IYSPTRIKYP MVRREFLEKG VNADRSTRGN 

       130        140        150        160        170        180 
GDFVRVTWDE ALDLVARELK RVQESYGPTG TFGGSYGWKS PGRLHNCQVL MRRALNLAGG 

       190        200        210        220        230        240 
FVNSSGDYST AAAQIIMPHV MGTLEVYEQQ TAWPVVVENT DLMVFWAADP MKTNEIGWVI 

       250        260        270        280        290        300 
PDHGAYAGMK ALKEKGTRVI CINPVRTETA DYFGADVVSP RPQTDVALML GMAHTLYSED 

       310        320        330        340        350        360 
LHDKDFLENC TTGFDLFAAY LTGESDGTPK TAEWAAEICG LPAEQIRELA RSFVAGRTML 

       370        380        390        400        410        420 
AAGWSIQRMH HGEQAHWMLV TLASMIGQIG LPGGGFGLSY HYSNGGSPTS DGPALGGISD 

       430        440        450        460        470        480 
GGKAVEGAAW LSESGATSIP CARVVDMLLN PGGEFQFNGA TATYPDVKLA YWAGGNPFAH 

       490        500        510        520        530        540 
HQDRNRMLKA WEKLETFIVQ DFQWTATARH ADIVLPATTS YERNDIESVG DYSNRAILAM 

       550        560        570        580        590        600 
KKVVDPLYEA RSDYDIFAAL AERLGKGAEF TEGRDEMGWI SSFYEAAVKQ AEFKNVAMPS 

       610        620        630        640        650        660 
FEDFWSEGIV EFPITEGANF VRYADFREDP LFNPLGTPSG LIEIYSKNIE KMGYDDCPAH 

       670        680        690        700        710        720 
PTWMEPAERL GGAGAKYPLH VVASHPKSRL HSQLNGTSLR DLYAVAGHEP CLINPADAAA 

       730        740        750        760        770        780 
RGIADGDVLR VFNDRGQILV GAKVSDAVMP GAIQIYEGGW YDPLDPSEEG TLDKYGDVNV 

       790        800        810        820 
LSLDVGTSKL AQGNCGQTIL ADVEKYAGAP VTVTVFDTPK GA

« Hide

References

[1]"Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter sphaeroides."
Hilton J.C., Rajagopalan K.V.
Biochim. Biophys. Acta 1294:111-114(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: f. sp. denitrificans IL106.
[2]"Cloning and nucleotide sequence of the gene encoding dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans."
Yamamoto I., Wada N., Ujiiye T., Tachibana M., Matsuzaki M., Kajiwara H., Watanabe Y., Hirano H., Okubo A., Satoh T., Yamazaki S.
Biosci. Biotechnol. Biochem. 59:1850-1855(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE.
Strain: f. sp. denitrificans IL106.
[3]"The amino acid sequence of Rhodobacter sphaeroides dimethyl sulfoxide reductase."
Barber M.J., van Valkenburgh H., Trimboli A.J., Pollock V.V., Neame P.J., Bastian N.R.
Arch. Biochem. Biophys. 320:266-275(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-815, PROTEIN SEQUENCE OF 43-815.
Strain: f. sp. denitrificans IL106.
[4]"Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans."
Johnson J.L., Bastian N.R., Rajagopalan K.V.
Proc. Natl. Acad. Sci. U.S.A. 87:3190-3194(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[5]"Molybdenum requirement for translocation of dimethyl sulfoxide reductase to the periplasmic space in a photodenitrifier, Rhodobacter sphaeroides f. sp. denitrificans."
Yoshida Y., Takai M., Satoh T., Takami S.
J. Bacteriol. 173:3277-3281(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, COFACTOR.
[6]"Characterization of genes encoding dimethyl sulfoxide reductase of Rhodobacter sphaeroides 2.4.1T: an essential metabolic gene function encoded on chromosome II."
Mouncey N.J., Choudhary M., Kaplan S.
J. Bacteriol. 179:7617-7624(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A DIMETHYL SULFOXIDE AND TRIMETHYLAMINE N-OXIDE REDUCTASE, DISRUPTION PHENOTYPE.
[7]"Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination."
Schindelin H., Kisker C., Hilton J., Rajagopalan K.V., Rees D.C.
Science 272:1615-1621(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COFACTOR.
[8]"The 1.3 A crystal structure of Rhodobacter sphaeroides dimethyl sulfoxide reductase reveals two distinct molybdenum coordination environments."
Li H.-K., Temple C., Rajagopalan K.V., Schindelin H.
J. Am. Chem. Soc. 122:7673-7680(2000)
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L46851 Genomic DNA. Translation: AAB07230.1.
D38634 Genomic DNA. Translation: BAA07615.1.
U25037 Genomic DNA. Translation: AAC13660.1.
PIRS70012.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EU1X-ray1.30A43-822[»]
ProteinModelPortalQ57366.
SMRQ57366. Positions 46-822.
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.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PfamPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR00509. bisC_fam. 1 hit.
TIGR01409. TAT_signal_seq. 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

EvolutionaryTraceQ57366.

Entry information

Entry nameDSTOR_RHOSH
AccessionPrimary (citable) accession number: Q57366
Secondary accession number(s): Q53077
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 90 of the entry and version 1 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