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Q57366

- DSTOR_RHOSH

UniProt

Q57366 - DSTOR_RHOSH

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Protein
Dimethyl sulfoxide/trimethylamine N-oxide reductase
Gene
dmsA, dsrA
Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581Molybdopterin guanine dinucleotide 2
Metal bindingi189 – 1891Molybdenum
Binding sitei368 – 3681Molybdopterin guanine dinucleotide 1
Binding sitei476 – 4761Molybdopterin guanine dinucleotide 1
Binding sitei480 – 4801Molybdopterin guanine dinucleotide 1
Binding sitei523 – 5231Molybdopterin guanine dinucleotide 1
Binding sitei553 – 5531Molybdopterin guanine dinucleotide 1
Binding sitei689 – 6891Molybdopterin guanine dinucleotide 1
Binding sitei779 – 7791Molybdopterin guanine dinucleotide 1

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. molybdenum ion binding Source: InterPro
  3. trimethylamine-N-oxide reductase (cytochrome c) activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, Molybdenum

    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:dmsA
    Synonyms:dsrA
    OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
    Taxonomic identifieri1063 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4242Tat-type signal2 Publications
    Add
    BLAST
    Chaini43 – 822780Dimethyl sulfoxide/trimethylamine N-oxide reductase
    PRO_0000019146Add
    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.1 Publication

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 547
    Beta strandi57 – 648
    Beta strandi67 – 737
    Helixi84 – 896
    Turni90 – 923
    Beta strandi101 – 1033
    Helixi104 – 1096
    Helixi110 – 1123
    Helixi115 – 1173
    Beta strandi123 – 1253
    Helixi128 – 14619
    Helixi148 – 1503
    Helixi167 – 17812
    Beta strandi182 – 1865
    Beta strandi188 – 1903
    Helixi193 – 2008
    Helixi213 – 2197
    Beta strandi221 – 2277
    Helixi230 – 2334
    Beta strandi238 – 2403
    Helixi244 – 25512
    Beta strandi258 – 2658
    Helixi268 – 2736
    Beta strandi276 – 2783
    Helixi285 – 29814
    Helixi304 – 3107
    Helixi314 – 3218
    Turni322 – 3265
    Helixi332 – 3398
    Helixi343 – 35412
    Beta strandi358 – 3625
    Helixi365 – 3673
    Turni370 – 3734
    Helixi374 – 38613
    Beta strandi395 – 3984
    Turni403 – 4064
    Beta strandi437 – 4404
    Helixi441 – 4433
    Helixi444 – 4496
    Beta strandi454 – 4574
    Beta strandi460 – 4634
    Beta strandi469 – 4746
    Helixi477 – 4804
    Helixi484 – 4907
    Helixi491 – 4933
    Beta strandi495 – 5039
    Helixi506 – 5094
    Beta strandi512 – 5176
    Helixi520 – 5223
    Beta strandi525 – 5295
    Turni531 – 5333
    Beta strandi536 – 5405
    Helixi553 – 56311
    Helixi567 – 5715
    Helixi576 – 59318
    Helixi601 – 6077
    Beta strandi609 – 6113
    Helixi616 – 6194
    Helixi624 – 6285
    Turni630 – 6323
    Beta strandi640 – 6456
    Helixi647 – 6526
    Beta strandi677 – 6826
    Beta strandi687 – 6904
    Turni694 – 6963
    Helixi698 – 7025
    Beta strandi710 – 7134
    Helixi715 – 7195
    Turni720 – 7223
    Beta strandi728 – 7325
    Beta strandi737 – 7448
    Beta strandi752 – 7543
    Beta strandi773 – 7753
    Helixi778 – 7803
    Turni789 – 7913
    Beta strandi800 – 8056

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EU1X-ray1.30A43-822[»]
    ProteinModelPortaliQ57366.
    SMRiQ57366. Positions 46-822.

    Miscellaneous databases

    EvolutionaryTraceiQ57366.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni158 – 1603MGD 1 binding
    Regioni232 – 2332MGD 2 binding
    Regioni262 – 2632MGD 2 binding
    Regioni283 – 2853MGD 2 binding
    Regioni364 – 3652MGD 2 binding
    Regioni500 – 5012MGD 1 binding
    Regioni683 – 6864MGD 1 binding
    Regioni691 – 6933MGD 1 binding
    Regioni796 – 7972MGD 1 binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    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.
    IPR019546. TAT_signal_bac_arc.
    [Graphical view]
    PfamiPF00384. Molybdopterin. 1 hit.
    PF01568. Molydop_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF50692. SSF50692. 1 hit.
    TIGRFAMsiTIGR00509. bisC_fam. 1 hit.
    TIGR01409. TAT_signal_seq. 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.

    Q57366-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKLSGQELH AELSRRAFLS YTAAVGALGL CGTSLLAQGA RAEGLANGEV    50
    MSGCHWGVFK ARVENGRAVA FEPWDKDPAP SHQLPGVLDS IYSPTRIKYP 100
    MVRREFLEKG VNADRSTRGN GDFVRVTWDE ALDLVARELK RVQESYGPTG 150
    TFGGSYGWKS PGRLHNCQVL MRRALNLAGG FVNSSGDYST AAAQIIMPHV 200
    MGTLEVYEQQ TAWPVVVENT DLMVFWAADP MKTNEIGWVI PDHGAYAGMK 250
    ALKEKGTRVI CINPVRTETA DYFGADVVSP RPQTDVALML GMAHTLYSED 300
    LHDKDFLENC TTGFDLFAAY LTGESDGTPK TAEWAAEICG LPAEQIRELA 350
    RSFVAGRTML AAGWSIQRMH HGEQAHWMLV TLASMIGQIG LPGGGFGLSY 400
    HYSNGGSPTS DGPALGGISD GGKAVEGAAW LSESGATSIP CARVVDMLLN 450
    PGGEFQFNGA TATYPDVKLA YWAGGNPFAH HQDRNRMLKA WEKLETFIVQ 500
    DFQWTATARH ADIVLPATTS YERNDIESVG DYSNRAILAM KKVVDPLYEA 550
    RSDYDIFAAL AERLGKGAEF TEGRDEMGWI SSFYEAAVKQ AEFKNVAMPS 600
    FEDFWSEGIV EFPITEGANF VRYADFREDP LFNPLGTPSG LIEIYSKNIE 650
    KMGYDDCPAH PTWMEPAERL GGAGAKYPLH VVASHPKSRL HSQLNGTSLR 700
    DLYAVAGHEP CLINPADAAA RGIADGDVLR VFNDRGQILV GAKVSDAVMP 750
    GAIQIYEGGW YDPLDPSEEG TLDKYGDVNV LSLDVGTSKL AQGNCGQTIL 800
    ADVEKYAGAP VTVTVFDTPK GA 822
    Length:822
    Mass (Da):89,208
    Last modified:November 1, 1996 - v1
    Checksum:i4AB3497E5D26B1C9
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851S → V in AAC13660. 1 Publication
    Sequence conflicti192 – 1921A → G in AAC13660. 1 Publication
    Sequence conflicti199 – 1991H → Y in AAC13660. 1 Publication
    Sequence conflicti371 – 3733HGE → MAQ in AAC13660. 1 Publication
    Sequence conflicti422 – 4221G → A in AAC13660. 1 Publication
    Sequence conflicti430 – 4301W → C in AAC13660. 1 Publication
    Sequence conflicti695 – 6951N → T in AAC13660. 1 Publication
    Sequence conflicti706 – 7061A → V in AAC13660. 1 Publication
    Sequence conflicti742 – 7421A → T in AAC13660. 1 Publication
    Sequence conflicti749 – 7491M → I in AAC13660. 1 Publication
    Sequence conflicti793 – 7931G → D in AAC13660. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L46851 Genomic DNA. Translation: AAB07230.1.
    D38634 Genomic DNA. Translation: BAA07615.1.
    U25037 Genomic DNA. Translation: AAC13660.1.
    PIRiS70012.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L46851 Genomic DNA. Translation: AAB07230.1 .
    D38634 Genomic DNA. Translation: BAA07615.1 .
    U25037 Genomic DNA. Translation: AAC13660.1 .
    PIRi S70012.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EU1 X-ray 1.30 A 43-822 [» ]
    ProteinModelPortali Q57366.
    SMRi Q57366. Positions 46-822.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q57366.

    Family and domain databases

    InterProi IPR009010. 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 ]
    Pfami PF00384. Molybdopterin. 1 hit.
    PF01568. Molydop_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50692. SSF50692. 1 hit.
    TIGRFAMsi TIGR00509. bisC_fam. 1 hit.
    TIGR01409. TAT_signal_seq. 1 hit.
    PROSITEi PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
    PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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) IN COMPLEX WITH MO-BIS-MGD, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiDSTOR_RHOSH
    AccessioniPrimary (citable) accession number: Q57366
    Secondary accession number(s): Q53077
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: September 3, 2014
    This is version 95 of the entry and version 1 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

    External Data

    Dasty 3

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