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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...

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 PublicationsAdd
BLAST
Chaini43 – 822780Dimethyl sulfoxide/trimethylamine N-oxide reductasePRO_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

1
822
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...
MobiDBi 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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