Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of MTND_KLEOX

EC Number:1.13.11.53

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
acireductone dioxygenase (Ni2+-requiring)
Q9ZFE7
Klebsiella oxytoca
180
20329
Reaction
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + formate + CO
Other sequences found for EC No. 1.13.11.53

EC Number:1.13.11.54

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
acireductone dioxygenase [iron(II)-requiring]
Q9ZFE7
Klebsiella oxytoca
180
20329
Reaction
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-(methylsulfanyl)-2-oxobutanoate + formate
Other sequences found for EC No. 1.13.11.54

General information:

Sequence
show sequence in fasta format
  0 MSALTIFSVK DPQNSLWHST NAEEIQQQLN AKGVRFERWQ ADRDLGAAPT AETVIAAYQH
 60 AIDKLVAEKG YQSWDVISLR ADNPQKEALR EKFLNEHTHG EDEVRFFVEG AGLFCLHIGD
120 EVFQVLCEKN DLISVPAHTP HWFDMGSEPN FTAIRIFDNP EGWIAQFTGD DIASAYPRLA
Download this sequence
in fasta format
Download all sequences for 1.13.11.54
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
321287
Balakrishnan R.,Frohlich M.,Rahaim P.T.,Backman K.,Yocum R.R.
Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca.
J. Biol. Chem.
268
24792-24795
1993
321288
Dai Y.,Wensink P.C.,Abeles R.H.
One protein, two enzymes.
J. Biol. Chem.
274
1193-1195
1999
321289
Wray J.W.,Abeles R.H.
A bacterial enzyme that catalyzes formation of carbon monoxide.
J. Biol. Chem.
268
21466-21469
1993
321290
Dai Y.,Pochapsky T.C.,Abeles R.H.
Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae.
Biochemistry
40
6379-6387
2001
321291
Chai S.C.,Ju T.,Dang M.,Goldsmith R.B.,Maroney M.J.,Pochapsky T.C.
Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724.
Biochemistry
47
2428-2438
2008
321292
Pochapsky T.C.,Pochapsky S.S.,Ju T.,Mo H.,Al-Mjeni F.,Maroney M.J.
Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae.
Nat. Struct. Biol.
9
966-972
2002
321293
Pochapsky T.C.,Pochapsky S.S.,Ju T.,Hoefler C.,Liang J.
A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings.
J. Biomol. NMR
34
117-127
2006
321294
Ju T.,Goldsmith R.B.,Chai S.C.,Maroney M.J.,Pochapsky S.S.,Pochapsky T.C.
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase.
J. Mol. Biol.
363
823-834
2006