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Q57366

- DSTOR_RHOSH

UniProt

Q57366 - DSTOR_RHOSH

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Protein

Dimethyl sulfoxide/trimethylamine N-oxide reductase

Gene

dmsA

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

Mo-bis(molybdopterin guanine dinucleotide)3 PublicationsNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.3 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-KW
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 PublicationsPROSITE-ProRule annotationAdd
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.2 Publications

Structurei

Secondary structure

1
822
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 – 896Combined sources
Turni90 – 923Combined 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
Helixi213 – 2197Combined sources
Beta strandi221 – 2277Combined sources
Helixi230 – 2334Combined sources
Beta strandi238 – 2403Combined sources
Helixi244 – 25512Combined sources
Beta strandi258 – 2658Combined sources
Helixi268 – 2736Combined sources
Beta strandi276 – 2783Combined sources
Helixi285 – 29814Combined sources
Helixi304 – 3107Combined sources
Helixi314 – 3218Combined sources
Turni322 – 3265Combined sources
Helixi332 – 3398Combined sources
Helixi343 – 35412Combined sources
Beta strandi358 – 3625Combined sources
Helixi365 – 3673Combined sources
Turni370 – 3734Combined sources
Helixi374 – 38613Combined sources
Beta strandi395 – 3984Combined sources
Turni403 – 4064Combined 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
Helixi616 – 6194Combined sources
Helixi624 – 6285Combined sources
Turni630 – 6323Combined sources
Beta strandi640 – 6456Combined sources
Helixi647 – 6526Combined sources
Beta strandi677 – 6826Combined sources
Beta strandi687 – 6904Combined sources
Turni694 – 6963Combined sources
Helixi698 – 7025Combined sources
Beta strandi710 – 7134Combined sources
Helixi715 – 7195Combined sources
Turni720 – 7223Combined 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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EU1X-ray1.30A43-822[»]
ProteinModelPortaliQ57366.
SMRiQ57366. Positions 46-822.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MTKLSGQELH AELSRRAFLS YTAAVGALGL CGTSLLAQGA RAEGLANGEV
60 70 80 90 100
MSGCHWGVFK ARVENGRAVA FEPWDKDPAP SHQLPGVLDS IYSPTRIKYP
110 120 130 140 150
MVRREFLEKG VNADRSTRGN GDFVRVTWDE ALDLVARELK RVQESYGPTG
160 170 180 190 200
TFGGSYGWKS PGRLHNCQVL MRRALNLAGG FVNSSGDYST AAAQIIMPHV
210 220 230 240 250
MGTLEVYEQQ TAWPVVVENT DLMVFWAADP MKTNEIGWVI PDHGAYAGMK
260 270 280 290 300
ALKEKGTRVI CINPVRTETA DYFGADVVSP RPQTDVALML GMAHTLYSED
310 320 330 340 350
LHDKDFLENC TTGFDLFAAY LTGESDGTPK TAEWAAEICG LPAEQIRELA
360 370 380 390 400
RSFVAGRTML AAGWSIQRMH HGEQAHWMLV TLASMIGQIG LPGGGFGLSY
410 420 430 440 450
HYSNGGSPTS DGPALGGISD GGKAVEGAAW LSESGATSIP CARVVDMLLN
460 470 480 490 500
PGGEFQFNGA TATYPDVKLA YWAGGNPFAH HQDRNRMLKA WEKLETFIVQ
510 520 530 540 550
DFQWTATARH ADIVLPATTS YERNDIESVG DYSNRAILAM KKVVDPLYEA
560 570 580 590 600
RSDYDIFAAL AERLGKGAEF TEGRDEMGWI SSFYEAAVKQ AEFKNVAMPS
610 620 630 640 650
FEDFWSEGIV EFPITEGANF VRYADFREDP LFNPLGTPSG LIEIYSKNIE
660 670 680 690 700
KMGYDDCPAH PTWMEPAERL GGAGAKYPLH VVASHPKSRL HSQLNGTSLR
710 720 730 740 750
DLYAVAGHEP CLINPADAAA RGIADGDVLR VFNDRGQILV GAKVSDAVMP
760 770 780 790 800
GAIQIYEGGW YDPLDPSEEG TLDKYGDVNV LSLDVGTSKL AQGNCGQTIL
810 820
ADVEKYAGAP VTVTVFDTPK GA
Length:822
Mass (Da):89,208
Last modified:November 1, 1996 - v1
Checksum:i4AB3497E5D26B1C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851S → V in AAC13660. (PubMed:7625833)Curated
Sequence conflicti192 – 1921A → G in AAC13660. (PubMed:7625833)Curated
Sequence conflicti199 – 1991H → Y in AAC13660. (PubMed:7625833)Curated
Sequence conflicti371 – 3733HGE → MAQ in AAC13660. (PubMed:7625833)Curated
Sequence conflicti422 – 4221G → A in AAC13660. (PubMed:7625833)Curated
Sequence conflicti430 – 4301W → C in AAC13660. (PubMed:7625833)Curated
Sequence conflicti695 – 6951N → T in AAC13660. (PubMed:7625833)Curated
Sequence conflicti706 – 7061A → V in AAC13660. (PubMed:7625833)Curated
Sequence conflicti742 – 7421A → T in AAC13660. (PubMed:7625833)Curated
Sequence conflicti749 – 7491M → I in AAC13660. (PubMed:7625833)Curated
Sequence conflicti793 – 7931G → D in AAC13660. (PubMed:7625833)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 98 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