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Dimethyl sulfoxide/trimethylamine N-oxide reductase (DMSO reductase) (DMSOR) (Me2SO reductase) (TMAOR) (EC 1.7.2.3) (EC 1.8.5.3)

 DSTOR_RHOSH             Reviewed;         822 AA.
Q57366; Q53077;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 110.
RecName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase;
Short=DMSO reductase;
Short=DMSOR;
Short=Me2SO reductase;
Short=TMAOR;
EC=1.7.2.3;
EC=1.8.5.3;
Flags: Precursor;
Name=dmsA; Synonyms=dsrA;
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Rhodobacter.
NCBI_TaxID=1063;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=f. sp. denitrificans IL106;
PubMed=8645727; DOI=10.1016/0167-4838(96)00015-5;
Hilton J.C., Rajagopalan K.V.;
"Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter
sphaeroides.";
Biochim. Biophys. Acta 1294:111-114(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
PARTIAL PROTEIN SEQUENCE.
STRAIN=f. sp. denitrificans IL106;
PubMed=8534974; DOI=10.1271/bbb.59.1850;
Yamamoto I., Wada N., Ujiiye T., Tachibana M., Matsuzaki M.,
Kajiwara H., Watanabe Y., Hirano H., Okubo A., Satoh T., Yamazaki S.;
"Cloning and nucleotide sequence of the gene encoding dimethyl
sulfoxide reductase from Rhodobacter sphaeroides f. sp.
denitrificans.";
Biosci. Biotechnol. Biochem. 59:1850-1855(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-815, AND PROTEIN SEQUENCE OF
43-815.
STRAIN=f. sp. denitrificans IL106;
PubMed=7625833; DOI=10.1016/0003-9861(95)90009-8;
Barber M.J., van Valkenburgh H., Trimboli A.J., Pollock V.V.,
Neame P.J., Bastian N.R.;
"The amino acid sequence of Rhodobacter sphaeroides dimethyl sulfoxide
reductase.";
Arch. Biochem. Biophys. 320:266-275(1995).
[4]
COFACTOR.
PubMed=2326278; DOI=10.1073/pnas.87.8.3190;
Johnson J.L., Bastian N.R., Rajagopalan K.V.;
"Molybdopterin guanine dinucleotide: a modified form of molybdopterin
identified in the molybdenum cofactor of dimethyl sulfoxide reductase
from Rhodobacter sphaeroides forma specialis denitrificans.";
Proc. Natl. Acad. Sci. U.S.A. 87:3190-3194(1990).
[5]
SUBCELLULAR LOCATION, AND COFACTOR.
PubMed=1710616; DOI=10.1128/jb.173.11.3277-3281.1991;
Yoshida Y., Takai M., Satoh T., Takami S.;
"Molybdenum requirement for translocation of dimethyl sulfoxide
reductase to the periplasmic space in a photodenitrifier, Rhodobacter
sphaeroides f. sp. denitrificans.";
J. Bacteriol. 173:3277-3281(1991).
[6]
FUNCTION AS A DIMETHYL SULFOXIDE AND TRIMETHYLAMINE N-OXIDE REDUCTASE,
AND DISRUPTION PHENOTYPE.
PubMed=9401017; DOI=10.1128/jb.179.24.7617-7624.1997;
Mouncey N.J., Choudhary M., Kaplan S.;
"Characterization of genes encoding dimethyl sulfoxide reductase of
Rhodobacter sphaeroides 2.4.1T: an essential metabolic gene function
encoded on chromosome II.";
J. Bacteriol. 179:7617-7624(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COFACTOR.
PubMed=8658134; DOI=10.1126/science.272.5268.1615;
Schindelin H., Kisker C., Hilton J., Rajagopalan K.V., Rees D.C.;
"Crystal structure of DMSO reductase: redox-linked changes in
molybdopterin coordination.";
Science 272:1615-1621(1996).
[8]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MO-BIS-MGD,
COFACTOR, AND SUBUNIT.
Li H.-K., Temple C., Rajagopalan K.V., Schindelin H.;
"The 1.3 A crystal structure of Rhodobacter sphaeroides dimethyl
sulfoxide reductase reveals two distinct molybdenum coordination
environments.";
J. Am. Chem. Soc. 122:7673-7680(2000).
-!- 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.
{ECO:0000269|PubMed:9401017}.
-!- CATALYTIC ACTIVITY: Dimethylsulfide + menaquinone + H(2)O =
dimethylsulfoxide + menaquinol.
-!- CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit
+ H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit +
2 H(+).
-!- COFACTOR:
Name=Mo-bis(molybdopterin guanine dinucleotide);
Xref=ChEBI:CHEBI:60539;
Evidence={ECO:0000269|PubMed:1710616,
ECO:0000269|PubMed:2326278, ECO:0000269|Ref.8};
Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
(Mo-bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:1710616,
ECO:0000269|PubMed:2326278, ECO:0000269|Ref.8};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8658134,
ECO:0000269|Ref.8}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1710616}.
-!- PTM: 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.
{ECO:0000269|PubMed:9401017}.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L46851; AAB07230.1; -; Genomic_DNA.
EMBL; D38634; BAA07615.1; -; Genomic_DNA.
EMBL; U25037; AAC13660.1; -; Genomic_DNA.
PIR; S70012; S70012.
PDB; 1EU1; X-ray; 1.30 A; A=43-822.
PDBsum; 1EU1; -.
ProteinModelPortal; Q57366; -.
SMR; Q57366; -.
DrugBank; DB02153; 3-Sulfinoalanine.
DrugBank; DB02379; Beta-D-Glucose.
eggNOG; ENOG4108J2R; Bacteria.
eggNOG; COG0243; LUCA.
EvolutionaryTrace; Q57366; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR006658; BisC.
InterPro; IPR006657; MoPterin_dinucl-bd_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
InterPro; IPR006311; TAT_signal.
InterPro; IPR019546; TAT_signal_bac_arc.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF01568; Molydop_binding; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR00509; bisC_fam; 1.
TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Metal-binding; Molybdenum;
Oxidoreductase; Periplasm; Signal.
SIGNAL 1 42 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648,
ECO:0000269|PubMed:7625833,
ECO:0000269|PubMed:8534974}.
CHAIN 43 822 Dimethyl sulfoxide/trimethylamine N-oxide
reductase.
/FTId=PRO_0000019146.
REGION 158 160 MGD 1 binding.
REGION 232 233 MGD 2 binding.
REGION 262 263 MGD 2 binding.
REGION 283 285 MGD 2 binding.
REGION 364 365 MGD 2 binding.
REGION 500 501 MGD 1 binding.
REGION 683 686 MGD 1 binding.
REGION 691 693 MGD 1 binding.
REGION 796 797 MGD 1 binding.
METAL 189 189 Molybdenum.
BINDING 158 158 Molybdopterin guanine dinucleotide 2.
BINDING 368 368 Molybdopterin guanine dinucleotide 1.
BINDING 476 476 Molybdopterin guanine dinucleotide 1.
BINDING 480 480 Molybdopterin guanine dinucleotide 1.
BINDING 523 523 Molybdopterin guanine dinucleotide 1.
BINDING 553 553 Molybdopterin guanine dinucleotide 1.
BINDING 689 689 Molybdopterin guanine dinucleotide 1.
BINDING 779 779 Molybdopterin guanine dinucleotide 1.
CONFLICT 185 185 S -> V (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 192 192 A -> G (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 199 199 H -> Y (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 371 373 HGE -> MAQ (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 422 422 G -> A (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 430 430 W -> C (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 695 695 N -> T (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 706 706 A -> V (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 742 742 A -> T (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 749 749 M -> I (in Ref. 3; AAC13660).
{ECO:0000305}.
CONFLICT 793 793 G -> D (in Ref. 3; AAC13660).
{ECO:0000305}.
STRAND 48 54 {ECO:0000244|PDB:1EU1}.
STRAND 57 64 {ECO:0000244|PDB:1EU1}.
STRAND 67 73 {ECO:0000244|PDB:1EU1}.
HELIX 84 89 {ECO:0000244|PDB:1EU1}.
TURN 90 92 {ECO:0000244|PDB:1EU1}.
STRAND 101 103 {ECO:0000244|PDB:1EU1}.
HELIX 104 109 {ECO:0000244|PDB:1EU1}.
HELIX 110 112 {ECO:0000244|PDB:1EU1}.
HELIX 115 117 {ECO:0000244|PDB:1EU1}.
STRAND 123 125 {ECO:0000244|PDB:1EU1}.
HELIX 128 146 {ECO:0000244|PDB:1EU1}.
HELIX 148 150 {ECO:0000244|PDB:1EU1}.
HELIX 167 178 {ECO:0000244|PDB:1EU1}.
STRAND 182 186 {ECO:0000244|PDB:1EU1}.
STRAND 188 190 {ECO:0000244|PDB:1EU1}.
HELIX 193 200 {ECO:0000244|PDB:1EU1}.
HELIX 213 219 {ECO:0000244|PDB:1EU1}.
STRAND 221 227 {ECO:0000244|PDB:1EU1}.
HELIX 230 233 {ECO:0000244|PDB:1EU1}.
STRAND 238 240 {ECO:0000244|PDB:1EU1}.
HELIX 244 255 {ECO:0000244|PDB:1EU1}.
STRAND 258 265 {ECO:0000244|PDB:1EU1}.
HELIX 268 273 {ECO:0000244|PDB:1EU1}.
STRAND 276 278 {ECO:0000244|PDB:1EU1}.
HELIX 285 298 {ECO:0000244|PDB:1EU1}.
HELIX 304 310 {ECO:0000244|PDB:1EU1}.
HELIX 314 321 {ECO:0000244|PDB:1EU1}.
TURN 322 326 {ECO:0000244|PDB:1EU1}.
HELIX 332 339 {ECO:0000244|PDB:1EU1}.
HELIX 343 354 {ECO:0000244|PDB:1EU1}.
STRAND 358 362 {ECO:0000244|PDB:1EU1}.
HELIX 365 367 {ECO:0000244|PDB:1EU1}.
TURN 370 373 {ECO:0000244|PDB:1EU1}.
HELIX 374 386 {ECO:0000244|PDB:1EU1}.
STRAND 395 398 {ECO:0000244|PDB:1EU1}.
TURN 403 406 {ECO:0000244|PDB:1EU1}.
STRAND 437 440 {ECO:0000244|PDB:1EU1}.
HELIX 441 443 {ECO:0000244|PDB:1EU1}.
HELIX 444 449 {ECO:0000244|PDB:1EU1}.
STRAND 454 457 {ECO:0000244|PDB:1EU1}.
STRAND 460 463 {ECO:0000244|PDB:1EU1}.
STRAND 469 474 {ECO:0000244|PDB:1EU1}.
HELIX 477 480 {ECO:0000244|PDB:1EU1}.
HELIX 484 490 {ECO:0000244|PDB:1EU1}.
HELIX 491 493 {ECO:0000244|PDB:1EU1}.
STRAND 495 503 {ECO:0000244|PDB:1EU1}.
HELIX 506 509 {ECO:0000244|PDB:1EU1}.
STRAND 512 517 {ECO:0000244|PDB:1EU1}.
HELIX 520 522 {ECO:0000244|PDB:1EU1}.
STRAND 525 529 {ECO:0000244|PDB:1EU1}.
TURN 531 533 {ECO:0000244|PDB:1EU1}.
STRAND 536 540 {ECO:0000244|PDB:1EU1}.
HELIX 553 563 {ECO:0000244|PDB:1EU1}.
HELIX 567 571 {ECO:0000244|PDB:1EU1}.
HELIX 576 593 {ECO:0000244|PDB:1EU1}.
HELIX 601 607 {ECO:0000244|PDB:1EU1}.
STRAND 609 611 {ECO:0000244|PDB:1EU1}.
HELIX 616 619 {ECO:0000244|PDB:1EU1}.
HELIX 624 628 {ECO:0000244|PDB:1EU1}.
TURN 630 632 {ECO:0000244|PDB:1EU1}.
STRAND 640 645 {ECO:0000244|PDB:1EU1}.
HELIX 647 652 {ECO:0000244|PDB:1EU1}.
STRAND 677 682 {ECO:0000244|PDB:1EU1}.
STRAND 687 690 {ECO:0000244|PDB:1EU1}.
TURN 694 696 {ECO:0000244|PDB:1EU1}.
HELIX 698 702 {ECO:0000244|PDB:1EU1}.
STRAND 710 713 {ECO:0000244|PDB:1EU1}.
HELIX 715 719 {ECO:0000244|PDB:1EU1}.
TURN 720 722 {ECO:0000244|PDB:1EU1}.
STRAND 728 732 {ECO:0000244|PDB:1EU1}.
STRAND 737 744 {ECO:0000244|PDB:1EU1}.
STRAND 752 754 {ECO:0000244|PDB:1EU1}.
STRAND 773 775 {ECO:0000244|PDB:1EU1}.
HELIX 778 780 {ECO:0000244|PDB:1EU1}.
TURN 789 791 {ECO:0000244|PDB:1EU1}.
STRAND 800 805 {ECO:0000244|PDB:1EU1}.
SEQUENCE 822 AA; 89208 MW; 4AB3497E5D26B1C9 CRC64;
MTKLSGQELH AELSRRAFLS YTAAVGALGL CGTSLLAQGA RAEGLANGEV MSGCHWGVFK
ARVENGRAVA FEPWDKDPAP SHQLPGVLDS IYSPTRIKYP MVRREFLEKG VNADRSTRGN
GDFVRVTWDE ALDLVARELK RVQESYGPTG TFGGSYGWKS PGRLHNCQVL MRRALNLAGG
FVNSSGDYST AAAQIIMPHV MGTLEVYEQQ TAWPVVVENT DLMVFWAADP MKTNEIGWVI
PDHGAYAGMK ALKEKGTRVI CINPVRTETA DYFGADVVSP RPQTDVALML GMAHTLYSED
LHDKDFLENC TTGFDLFAAY LTGESDGTPK TAEWAAEICG LPAEQIRELA RSFVAGRTML
AAGWSIQRMH HGEQAHWMLV TLASMIGQIG LPGGGFGLSY HYSNGGSPTS DGPALGGISD
GGKAVEGAAW LSESGATSIP CARVVDMLLN PGGEFQFNGA TATYPDVKLA YWAGGNPFAH
HQDRNRMLKA WEKLETFIVQ DFQWTATARH ADIVLPATTS YERNDIESVG DYSNRAILAM
KKVVDPLYEA RSDYDIFAAL AERLGKGAEF TEGRDEMGWI SSFYEAAVKQ AEFKNVAMPS
FEDFWSEGIV EFPITEGANF VRYADFREDP LFNPLGTPSG LIEIYSKNIE KMGYDDCPAH
PTWMEPAERL GGAGAKYPLH VVASHPKSRL HSQLNGTSLR DLYAVAGHEP CLINPADAAA
RGIADGDVLR VFNDRGQILV GAKVSDAVMP GAIQIYEGGW YDPLDPSEEG TLDKYGDVNV
LSLDVGTSKL AQGNCGQTIL ADVEKYAGAP VTVTVFDTPK GA


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