Cysteine desulfurase_ (P77444)

Identification
Name:Cysteine desulfurase_
Synonyms:
  • Selenocysteine beta-lyase
  • SCL
  • Selenocysteine lyase
  • Selenocysteine reductase
Gene Name:sufS
Enzyme Class:
Biological Properties
General Function:Involved in metabolic process
Specific Function:Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Reduced acceptor ↔ 1.0Thumb+1.0Thumb+1.0Acceptor
1.0Selenocysteine + 1.0Reduced acceptor ↔ 1.0Hydrogen selenide + 1.0L-Alanine + 1.0Acceptor
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Methaneselenol
1.0Se-Methylselenocysteine + 1.0Water ↔ 1.0Pyruvic acid + 1.0Ammonia + 1.0Methaneselenol
ReactionCard
Complex Reactions:
1.0Thumb+1.0SufSE sulfur acceptor complex → 1.0Thumb+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 sulfur → 1.0Thumb+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 sulfur → 1.0Thumb+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 sulfur → 1.0Thumb+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
1.0Thumb+1.0reduced acceptor → 1.0Thumb+1.0Thumb+1.0acceptor
1.0Selenocysteine + 1.0reduced acceptor → 1.0Hydrogen selenide + 1.0L-Alanine + 1.0acceptor
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB11110Hydrogen selenideMetaboCard
ECMDB00692IronMetaboCard
ECMDB00161L-AlanineMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB21009Se-MethylselenocysteineMetaboCard
ECMDB03288SelenocysteineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
cysteine desulfurase activity
pyridoxal phosphate binding
sulfurtransferase activity
transferase activity
transferase activity, transferring sulfur-containing groups
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
cysteine metabolic process
metabolic process
sulfur amino acid metabolic process
Gene Properties
Blattner:b1680
Gene OrientationCounterclockwise
Centisome Percentage:37.88
Left Sequence End1757327
Right Sequence End1758547
Gene Sequence:
>1221 bp
ATGATTTTTTCCGTCGACAAAGTGCGGGCCGACTTTCCGGTGCTTTCGCGTGAGGTAAAC
GGTTTGCCGCTGGCTTATCTCGACAGCGCCGCCAGTGCGCAGAAACCGAGCCAGGTGATT
GACGCCGAGGCCGAGTTTTATCGTCATGGCTACGCGGCGGTGCATCGTGGTATTCATACC
TTAAGCGCCCAGGCGACCGAGAAAATGGAGAACGTGCGCAAGCGGGCATCGCTGTTTATT
AATGCCCGTTCGGCGGAAGAGCTGGTGTTCGTCCGCGGCACGACGGAAGGGATCAATCTG
GTCGCCAATAGCTGGGGCAACAGCAACGTGCGGGCGGGCGATAACATCATCATCAGTCAG
ATGGAGCACCACGCTAACATTGTTCCCTGGCAGATGCTTTGCGCACGCGTTGGCGCAGAG
CTGCGTGTGATCCCGCTCAATCCCGATGGTACGTTGCAACTGGAGACGCTGCCTACGCTG
TTTGATGAGAAAACTCGCCTGCTGGCAATTACTCATGTCTCCAACGTGCTTGGCACAGAA
AATCCACTGGCGGAAATGATCACGCTTGCGCACCAGCATGGCGCAAAAGTGCTGGTGGAT
GGCGCTCAGGCGGTGATGCATCATCCGGTGGATGTTCAGGCGCTGGATTGCGACTTTTAC
GTGTTCTCCGGGCATAAACTGTATGGCCCCACCGGAATTGGCATTCTTTATGTGAAAGAA
GCCTTGTTGCAGGAGATGCCGCCGTGGGAAGGGGGCGGTTCTATGATCGCCACCGTCAGC
CTGAGTGAAGGCACTACCTGGACCAAAGCACCATGGCGGTTTGAAGCCGGTACACCCAAT
ACCGGGGGCATCATTGGTCTTGGCGCGGCGCTGGAGTATGTTTCGGCGCTGGGGCTTAAT
AACATAGCCGAGTATGAACAGAATCTGATGCATTATGCGCTATCACAGCTGGAATCTGTA
CCGGATCTCACTCTCTATGGCCCACAAAACAGGCTTGGCGTTATTGCTTTTAATCTCGGT
AAACACCACGCCTATGATGTTGGCAGTTTTCTCGATAATTACGGCATTGCTGTGCGTACC
GGACATCACTGCGCAATGCCATTGATGGCCTATTACAACGTCCCTGCGATGTGTCGGGCG
TCGCTGGCCATGTATAACACCCATGAAGAAGTGGATCGTCTGGTGACCGGCCTGCAACGT
ATTCACCGTTTGCTGGGATAA
Protein Properties
Pfam Domain Function:
Protein Residues:406
Protein Molecular Weight:44433
Protein Theoretical pI:6
PDB File:1I29
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cysteine desulfurase
MIFSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHT
LSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQ
MEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTE
NPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE
ALLQEMPPWEGGGSMIATVSLSEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLN
NIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRT
GHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIHRLLG
References
External Links:
ResourceLink
Uniprot ID:P77444
Uniprot Name:SUFS_ECOLI
GenBank Gene ID:AB055108
Genebank Protein ID:12619308
PDB ID:1I29
Ecogene ID:EG13962
Ecocyc:EG13962
ColiBase:b1680
Kegg Gene:b1680
EchoBASE ID:EB3720
CCDB:SUFS_ECOLI
BacMap:16129636
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Fujii, T., Maeda, M., Mihara, H., Kurihara, T., Esaki, N., Hata, Y. (2000). "Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase." Biochemistry 39:1263-1273. Pubmed: 10684605
  • 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
  • Lacourciere, G. M., Mihara, H., Kurihara, T., Esaki, N., Stadtman, T. C. (2000). "Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate." J Biol Chem 275:23769-23773. Pubmed: 10829016
  • Lima, C. D. (2002). "Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation." J Mol Biol 315:1199-1208. Pubmed: 11827487
  • 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
  • Mihara, H., Fujii, T., Kato, S., Kurihara, T., Hata, Y., Esaki, N. (2002). "Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine." J Biochem 131:679-685. Pubmed: 11983074
  • Mihara, H., Kato, S., Lacourciere, G. M., Stadtman, T. C., Kennedy, R. A., Kurihara, T., Tokumoto, U., Takahashi, Y., Esaki, N. (2002). "The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H." Proc Natl Acad Sci U S A 99:6679-6683. Pubmed: 11997471
  • Mihara, H., Kurihara, T., Yoshimura, T., Esaki, N. (2000). "Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions." J Biochem 127:559-567. Pubmed: 10739946
  • Mihara, H., Maeda, M., Fujii, T., Kurihara, T., Hata, Y., Esaki, N. (1999). "A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary x-ray crystallographic studies." J Biol Chem 274:14768-14772. Pubmed: 10329673
  • 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
  • Takahashi, Y., Tokumoto, U. (2002). "A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids." J Biol Chem 277:28380-28383. Pubmed: 12089140