Identification
Name:Cysteine desulfuration protein sufE
Synonyms:Not Available
Gene Name:sufE
Enzyme Class:Not Available
Biological Properties
General Function:Not Available
Specific Function:Participates in cysteine desulfuration mediated by sufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for sufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of sufS, an intermediate product of cysteine desulfuration process. Together with the sufBCD complex, it thereby enhances up to 50- fold, the cysteine desulfurase activity of sufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of sufS
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0Thumb+1.0SufSE sulfur acceptor complex1.0Thumb+1.0SufSE with bound sulfur
1.0L-Cysteine + 1.0SufSE sulfur acceptor complex → 1.0L-Alanine + 1.0SufSE with bound sulfur
ReactionCard
1.0[2Fe-1S] desulfurated iron-sulfur cluster+1.0Thumb+1.0Thumb+1.0SufBCD scaffold complex+1.0SufSE with bound sulfur1.0Thumb+5.0Thumb+1.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster+1.0SufSE sulfur acceptor complex
1.0[2Fe-1S] desulfurated iron-sulfur cluster + 1.0Adenosine triphosphate + 1.0Water + 1.0SufBCD scaffold complex + 1.0SufSE with bound sulfur → 1.0ADP + 5.0Hydrogen ion + 1.0Phosphate + 1.0SufBCD with bound [2Fe-2S] cluster + 1.0SufSE sulfur acceptor complex
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0SufBCD scaffold complex+2.0SufSE with bound sulfur1.0Thumb+1.0Thumb+7.0Thumb+1.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster+2.0SufSE sulfur acceptor complex
1.0Adenosine triphosphate + 1.0FADH2 + 2.0Iron + 1.0Water + 1.0SufBCD scaffold complex + 2.0SufSE with bound sulfur → 1.0ADP + 1.0FAD + 7.0Hydrogen ion + 1.0Phosphate + 1.0SufBCD with bound [2Fe-2S] cluster + 2.0SufSE sulfur acceptor complex
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster+2.0SufSE with bound sulfur1.0Thumb+1.0Thumb+7.0Thumb+1.0Thumb+1.0SufBCD with two bound [2Fe-2S] clusters+2.0SufSE sulfur acceptor complex
1.0Adenosine triphosphate + 1.0FADH2 + 2.0Iron + 1.0Water + 1.0SufBCD with bound [2Fe-2S] cluster + 2.0SufSE with bound sulfur → 1.0ADP + 1.0FAD + 7.0Hydrogen ion + 1.0Phosphate + 1.0SufBCD with two bound [2Fe-2S] clusters + 2.0SufSE sulfur acceptor complex
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00692IronMetaboCard
ECMDB00161L-AlanineMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:Not Available
Gene Properties
Blattner:b1679
Gene OrientationCounterclockwise
Centisome Percentage:37.87
Left Sequence End1756898
Right Sequence End1757314
Gene Sequence:
>417 bp
ATGCTCGATAAGCTCGACGCCGCCTTACGTTTTCAACAAGAGGCGCTCAATCTGCGCGCC
CAGCGTCAGGAAGTGCTGGCAGCAAACATCGCCAATGCCGATACCCCTGGTTATCAGGCG
CGCGATATCGATTTTGCCAGTGAACTTAAAAAAGTCATGCAACGTGGACGGGATGCAACC
AGTGTGGTTGCACTGACGATGACCTCAACGCAACACATTCCGGCGCAGGCGCTGACGCCT
CCTACCGCAGAACTGCAATACCGTATTCCGGACCAGCCTTCGCTTGACGGTAATACCGTC
GATATGGATCGCGAACGCACCCAGTTTGCCGATAACAGCCTGCAATACCAGATGAGCCTT
AGCGCGTTGAGCGGGCAAATCAAAGGCATGATGAACGTTTTACAGAGCGGAAATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:138
Protein Molecular Weight:15800
Protein Theoretical pI:6
PDB File:1MZG
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cysteine desulfuration protein sufE
MALLPDKEKLLRNFLRCANWEEKYLYIIELGQRLPELRDEDRSPQNSIQGCQSQVWIVMR
QNAQGIIELQGDSDAAIVKGLIAVVFILYDQMTPQDIVNFDVRPWFEKMALTQHLTPSRS
QGLEAMIRAIRAKAAALS
References
External Links:
ResourceLink
Uniprot ID:P76194
Uniprot Name:SUFE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062650
PDB ID:1MZG
Ecogene ID:EG13961
Ecocyc:EG13961
ColiBase:b1679
Kegg Gene:b1679
EchoBASE ID:EB3719
CCDB:SUFE_ECOLI
BacMap:16129635
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Goldsmith-Fischman, S., Kuzin, A., Edstrom, W. C., Benach, J., Shastry, R., Xiao, R., Acton, T. B., Honig, B., Montelione, G. T., Hunt, J. F. (2004). "The SufE sulfur-acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes." J Mol Biol 344:549-565. Pubmed: 15522304
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Loiseau, L., Ollagnier-de-Choudens, S., Nachin, L., Fontecave, M., Barras, F. (2003). "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase." J Biol Chem 278:38352-38359. Pubmed: 12876288
  • Ollagnier-de-Choudens, S., Lascoux, D., Loiseau, L., Barras, F., Forest, E., Fontecave, M. (2003). "Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE." FEBS Lett 555:263-267. Pubmed: 14644425
  • Outten, F. W., Wood, M. J., Munoz, F. M., Storz, G. (2003). "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli." J Biol Chem 278:45713-45719. Pubmed: 12941942
  • Patzer, S. I., Hantke, K. (1999). "SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli." J Bacteriol 181:3307-3309. Pubmed: 10322040