Sequence of DSTOR_RHOCA
EC Number:1.8.5.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
Other sequences found for EC No. 1.8.5.3
General information:
Sequence
0 MTKFSGNELR AELYRRAFLS YSVAPGALGM FGRSLLAKGA RAEALANGTV MSGSHWGVFT
60 ATVENGRATA FTPWEKDPHP TPMLEGVLDS IYSPTRIKYP MVRREFLEKG VNADRSTRGN
120 GDFVRVSWDQ ALDLVAAEVK RVEETYGPQG VFGGSYGWKS PGRLHNCTTL LRRMLTLAGG
180 YVNGAGDYST GAAQVIMPHV VGTLEVYEQQ TAWPVLAENT EVMVFWAADP IKTSQIGWVI
240 PEHGAYPGLE ALKAKGTKVI VIDPVRTKTV EFFGADHVTP KPQTDVAIML GMAHTLVAED
300 LYDKDFIANY TSGFDKFLPY LMGETDSTPK TAEWASDISG VPAETIKELA RLFISKRTML
360 AAGWSMQRMH HGEQAHWMLV TLASMLGQIG LPGGGFGLSY HYSGGGTPST SGPALSGITD
420 GGAATKGPEW LAASGASVIP VARVVDMLEN PGAEFDFNGT RSKFPDVKMA YWVGGNPFVH
480 HQDRNRMVKA WEKLETFIVH DFQWTPTARH ADIVLPATTS YERNDIETIG DYSNTGILAM
540 KKIVEPLYEA RSDYDIFAAV AERLGKGKEF TEGKDEMGWI KSFYDDAAKQ GKAGGVEMPA
600 FDAFWAEGIV EFPVTDGADF VRYASFREDP LLNPLGTPTG LIEIYSKNIE KMGYDDCPAH
660 PTWMEPLERL DGPGAKYPLH IAASHPFNRL HSQLNGTVLR EGYAVQGHEP CLMHPDDAAA
720 RGIADGDVVR VHNDRGQILT GVKVTDAVMK GVIQIYEGGW YDPSDVTEPG TLDKYGDVNV
780 LSADIGTSKL AQGNCGQTVL AEVEKYTGPA VTLTGFVAPK AAE
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
27623
Shaw A.L.,Hanson G.R.,McEwan A.G.
Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus.
Biochim. Biophys. Acta
1276
176-180
1996
27625
Knaeblein J.,Mann K.,Ehlert S.,Fonstein M.,Huber R.,Schneider F.
Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus.
J. Mol. Biol.
263
40-52
1996
27626
McEwan A.G.,Ferguson S.J.,Jackson J.B.
Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.
Biochem. J.
274
305-307
1991
27627
Schneider F.,Loewe J.,Huber R.,Schindelin H.,Kisker C.,Knaeblein J.
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88-A resolution.
J. Mol. Biol.
263
53-69
1996
27629
McAlpine A.S.,McEwan A.G.,Bailey S.
The high resolution crystal structure of DMSO reductase in complex with DMSO.
J. Mol. Biol.
275
613-623
1998
27630
Bray R.C.,Adams B.,Smith A.T.,Bennett B.,Bailey S.
Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family.
Biochemistry
39
11258-11269
2000
27631
Stewart L.J.,Bailey S.,Bennett B.,Charnock J.M.,Garner C.D.,McAlpine A.S.
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site.
J. Mol. Biol.
299
593-600
2000
27632
Bray R.C.,Adams B.,Smith A.T.,Richards R.L.,Lowe D.J.,Bailey S.
Reactions of dimethylsulfoxide reductase in the presence of dimethyl sulfide and the structure of the dimethyl sulfide-modified enzyme.
Biochemistry
40
9810-9820
2001
