Sequence of DFX_DESVH
EC Number:1.15.1.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
superoxide reductase
P20418
Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough)
126
13983
Reaction
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
Other sequences found for EC No. 1.15.1.2
General information:
Sequence
0 MPNQYEIYKC IHCGNIVEVL HAGGGDLVCC GEPMKLMKEG TSDGAKEKHV PVIEKTANGY
60 KVTVGSVAHP MEEKHWIEWI ELVADGVSYK KFLKPGDAPE AEFCIKADKV VAREYCNLHG
120 HWKAEA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
662673
Brumlik M.J.,Voordouw G.
Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough.
J. Bacteriol.
171
4996-5004
1989
662674
Heidelberg J.F.,Seshadri R.,Haveman S.A.,Hemme C.L.,Paulsen I.T.,Kolonay J.F.,Eisen J.A.,Ward N.L.,Methe B.A.,Brinkac L.M.,Daugherty S.C.,DeBoy R.T.,Dodson R.J.,Durkin A.S.,Madupu R.,Nelson W.C.,Sullivan S.A.,Fouts D.E.,Haft D.H.,Selengut J.,Peterson J.D.,Davidsen T.M.,Zafar N.,Zhou L.,Radune D.,Dimitrov G.,Hance M.,Tran K.,Khouri H.M.,Gill J.,Utterback T.R.,Feldblyum T.V.,Wall J.D.,Voordouw G.,Fraser C.M.
The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough.
Nat. Biotechnol.
22
554-559
2004
662675
Moura I.,Tavares P.,Moura J.J.G.,Ravi N.,Huynh B.H.,Liu M.-Y.,Le Gall J.
Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center.
J. Biol. Chem.
265
21596-21602
1990
662676
Verhagen M.F.J.M.,Voorhorst W.G.B.,Kolkman J.A.,Wolbert R.B.G.,Hagen W.R.
On the two iron centers of desulfoferrodoxin.
FEBS Lett.
336
13-18
1993
662677
Voordouw J.K.,Voordouw G.
Deletion of the rbo gene increases the oxygen sensitivity of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough.
Appl. Environ. Microbiol.
64
2882-2887
1998
662678
Emerson J.P.,Coulter E.D.,Cabelli D.E.,Phillips R.S.,Kurtz D.M. Jr.
Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris.
Biochemistry
41
4348-4357
2002
662679
Emerson J.P.,Coulter E.D.,Phillips R.S.,Kurtz D.M. Jr.
Kinetics of the superoxide reductase catalytic cycle.
J. Biol. Chem.
278
39662-39668
2003
662680
Clay M.D.,Emerson J.P.,Coulter E.D.,Kurtz D.M. Jr.,Johnson M.K.
Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris.
J. Biol. Inorg. Chem.
8
671-682
2003
662681
Emerson J.P.,Cabelli D.E.,Kurtz D.M. Jr.
An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo.
Proc. Natl. Acad. Sci. U.S.A.
100
3802-3807
2003
