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Protein

Dimethyl sulfoxide/trimethylamine N-oxide reductase

Gene

dmsA

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
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.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)DescriptionActionsGraphical viewLength
Binding sitei158Molybdopterin guanine dinucleotide 21
Metal bindingi189Molybdenum1
Binding sitei368Molybdopterin guanine dinucleotide 11
Binding sitei476Molybdopterin guanine dinucleotide 11
Binding sitei480Molybdopterin guanine dinucleotide 11
Binding sitei523Molybdopterin guanine dinucleotide 11
Binding sitei553Molybdopterin guanine dinucleotide 11
Binding sitei689Molybdopterin guanine dinucleotide 11
Binding sitei779Molybdopterin guanine dinucleotide 11

GO - Molecular functioni

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

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Tat-type signalPROSITE-ProRule annotation2 PublicationsAdd BLAST42
ChainiPRO_000001914643 – 822Dimethyl sulfoxide/trimethylamine N-oxide reductaseAdd BLAST780

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

Protein-protein interaction databases

STRINGi272943.RSP_3048.

Structurei

Secondary structure

1822
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 54Combined sources7
Beta strandi57 – 64Combined sources8
Beta strandi67 – 73Combined sources7
Helixi84 – 89Combined sources6
Turni90 – 92Combined sources3
Beta strandi101 – 103Combined sources3
Helixi104 – 109Combined sources6
Helixi110 – 112Combined sources3
Helixi115 – 117Combined sources3
Beta strandi123 – 125Combined sources3
Helixi128 – 146Combined sources19
Helixi148 – 150Combined sources3
Helixi167 – 178Combined sources12
Beta strandi182 – 186Combined sources5
Beta strandi188 – 190Combined sources3
Helixi193 – 200Combined sources8
Helixi213 – 219Combined sources7
Beta strandi221 – 227Combined sources7
Helixi230 – 233Combined sources4
Beta strandi238 – 240Combined sources3
Helixi244 – 255Combined sources12
Beta strandi258 – 265Combined sources8
Helixi268 – 273Combined sources6
Beta strandi276 – 278Combined sources3
Helixi285 – 298Combined sources14
Helixi304 – 310Combined sources7
Helixi314 – 321Combined sources8
Turni322 – 326Combined sources5
Helixi332 – 339Combined sources8
Helixi343 – 354Combined sources12
Beta strandi358 – 362Combined sources5
Helixi365 – 367Combined sources3
Turni370 – 373Combined sources4
Helixi374 – 386Combined sources13
Beta strandi395 – 398Combined sources4
Turni403 – 406Combined sources4
Beta strandi437 – 440Combined sources4
Helixi441 – 443Combined sources3
Helixi444 – 449Combined sources6
Beta strandi454 – 457Combined sources4
Beta strandi460 – 463Combined sources4
Beta strandi469 – 474Combined sources6
Helixi477 – 480Combined sources4
Helixi484 – 490Combined sources7
Helixi491 – 493Combined sources3
Beta strandi495 – 503Combined sources9
Helixi506 – 509Combined sources4
Beta strandi512 – 517Combined sources6
Helixi520 – 522Combined sources3
Beta strandi525 – 529Combined sources5
Turni531 – 533Combined sources3
Beta strandi536 – 540Combined sources5
Helixi553 – 563Combined sources11
Helixi567 – 571Combined sources5
Helixi576 – 593Combined sources18
Helixi601 – 607Combined sources7
Beta strandi609 – 611Combined sources3
Helixi616 – 619Combined sources4
Helixi624 – 628Combined sources5
Turni630 – 632Combined sources3
Beta strandi640 – 645Combined sources6
Helixi647 – 652Combined sources6
Beta strandi677 – 682Combined sources6
Beta strandi687 – 690Combined sources4
Turni694 – 696Combined sources3
Helixi698 – 702Combined sources5
Beta strandi710 – 713Combined sources4
Helixi715 – 719Combined sources5
Turni720 – 722Combined sources3
Beta strandi728 – 732Combined sources5
Beta strandi737 – 744Combined sources8
Beta strandi752 – 754Combined sources3
Beta strandi773 – 775Combined sources3
Helixi778 – 780Combined sources3
Turni789 – 791Combined sources3
Beta strandi800 – 805Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ57366.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 160MGD 1 binding3
Regioni232 – 233MGD 2 binding2
Regioni262 – 263MGD 2 binding2
Regioni283 – 285MGD 2 binding3
Regioni364 – 365MGD 2 binding2
Regioni500 – 501MGD 1 binding2
Regioni683 – 686MGD 1 binding4
Regioni691 – 693MGD 1 binding3
Regioni796 – 797MGD 1 binding2

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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti185S → V in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti192A → G in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti199H → Y in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti371 – 373HGE → MAQ in AAC13660 (PubMed:7625833).Curated3
Sequence conflicti422G → A in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti430W → C in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti695N → T in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti706A → V in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti742A → T in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti749M → I in AAC13660 (PubMed:7625833).Curated1
Sequence conflicti793G → D in AAC13660 (PubMed:7625833).Curated1

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.
PIRiS70012.

3D structure databases

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

Protein-protein interaction databases

STRINGi272943.RSP_3048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108J2R. Bacteria.
COG0243. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ57366.

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]
ProtoNetiSearch...

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 30, 2016
This is version 105 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

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.