Cysteine desulfurase
Details
- Name
- Cysteine desulfurase
- Synonyms
- 2.8.1.7
- csdB
- SCL
- Selenocysteine beta-lyase
- Selenocysteine lyase
- Selenocysteine reductase
- ynhB
- Gene Name
- sufS
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016459|Cysteine desulfurase MIFSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHT LSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQ MEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTE NPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE ALLQEMPPWEGGGSMIATVSLSEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLN NIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRT GHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIHRLLG
- Number of residues
- 406
- Molecular Weight
- 44433.435
- Theoretical pI
- 6.32
- GO Classification
- Functionscysteine desulfurase activity / pyridoxal phosphate binding / selenocysteine lyase activityProcessescysteine metabolic process / iron-sulfur cluster assembly / selenium compound metabolic process / sulfur compound metabolic process / sulfur incorporation into metallo-sulfur clusterComponentscytoplasm
- General Function
- Selenocysteine lyase activity
- 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.
- Pfam Domain Function
- Aminotran_5 (PF00266)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016460|Cysteine desulfurase (sufS) ATGATTTTTTCCGTCGACAAAGTGCGGGCCGACTTTCCGGTGCTTTCGCGTGAGGTAAAC GGTTTGCCGCTGGCTTATCTCGACAGCGCCGCCAGTGCGCAGAAACCGAGCCAGGTGATT GACGCCGAGGCCGAGTTTTATCGTCATGGCTACGCGGCGGTGCATCGTGGTATTCATACC TTAAGCGCCCAGGCGACCGAGAAAATGGAGAACGTGCGCAAGCGGGCATCGCTGTTTATT AATGCCCGTTCGGCGGAAGAGCTGGTGTTCGTCCGCGGCACGACGGAAGGGATCAATCTG GTCGCCAATAGCTGGGGCAACAGCAACGTGCGGGCGGGCGATAACATCATCATCAGTCAG ATGGAGCACCACGCTAACATTGTTCCCTGGCAGATGCTTTGCGCACGCGTTGGCGCAGAG CTGCGTGTGATCCCGCTCAATCCCGATGGTACGTTGCAACTGGAGACGCTGCCTACGCTG TTTGATGAGAAAACTCGCCTGCTGGCAATTACTCATGTCTCCAACGTGCTTGGCACAGAA AATCCACTGGCGGAAATGATCACGCTTGCGCACCAGCATGGCGCAAAAGTGCTGGTGGAT GGCGCTCAGGCGGTGATGCATCATCCGGTGGATGTTCAGGCGCTGGATTGCGACTTTTAC GTGTTCTCCGGGCATAAACTGTATGGCCCCACCGGAATTGGCATTCTTTATGTGAAAGAA GCCTTGTTGCAGGAGATGCCGCCGTGGGAAGGGGGCGGTTCTATGATCGCCACCGTCAGC CTGAGTGAAGGCACTACCTGGACCAAAGCACCATGGCGGTTTGAAGCCGGTACACCCAAT ACCGGGGGCATCATTGGTCTTGGCGCGGCGCTGGAGTATGTTTCGGCGCTGGGGCTTAAT AACATAGCCGAGTATGAACAGAATCTGATGCATTATGCGCTATCACAGCTGGAATCTGTA CCGGATCTCACTCTCTATGGCCCACAAAACAGGCTTGGCGTTATTGCTTTTAATCTCGGT AAACACCACGCCTATGATGTTGGCAGTTTTCTCGATAATTACGGCATTGCTGTGCGTACC GGACATCACTGCGCAATGCCATTGATGGCCTATTACAACGTCCCTGCGATGTGTCGGGCG TCGCTGGCCATGTATAACACCCATGAAGAAGTGGATCGTCTGGTGACCGGCCTGCAACGT ATTCACCGTTTGCTGGGATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P77444 UniProtKB Entry Name SUFS_ECOLI GenBank Protein ID 12619308 GenBank Gene ID AB055108 - General References
- Mihara H, Maeda M, Fujii T, Kurihara T, Hata Y, Esaki N: 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. 1999 May 21;274(21):14768-72. [Article]
- 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 al.: 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. 1996 Dec 31;3(6):363-77. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Patzer SI, Hantke K: SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J Bacteriol. 1999 May;181(10):3307-9. [Article]
- Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC: Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem. 2000 Aug 4;275(31):23769-73. [Article]
- Mihara H, Kurihara T, Yoshimura T, Esaki N: Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J Biochem. 2000 Apr;127(4):559-67. [Article]
- Takahashi Y, Tokumoto U: A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem. 2002 Aug 9;277(32):28380-3. Epub 2002 Jun 27. [Article]
- Mihara H, Kato S, Lacourciere GM, Stadtman TC, Kennedy RA, Kurihara T, Tokumoto U, Takahashi Y, Esaki N: 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. 2002 May 14;99(10):6679-83. Epub 2002 May 7. [Article]
- Loiseau L, Ollagnier-de-Choudens S, Nachin L, Fontecave M, Barras F: Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem. 2003 Oct 3;278(40):38352-9. Epub 2003 Jul 21. [Article]
- Outten FW, Wood MJ, Munoz FM, Storz G: 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. 2003 Nov 14;278(46):45713-9. Epub 2003 Aug 26. [Article]
- Ollagnier-de-Choudens S, Lascoux D, Loiseau L, Barras F, Forest E, Fontecave M: Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE. FEBS Lett. 2003 Dec 4;555(2):263-7. [Article]
- Fujii T, Maeda M, Mihara H, Kurihara T, Esaki N, Hata Y: Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry. 2000 Feb 15;39(6):1263-73. [Article]
- Mihara H, Fujii T, Kato S, Kurihara T, Hata Y, Esaki N: Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine. J Biochem. 2002 May;131(5):679-85. [Article]
- Lima CD: 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. 2002 Feb 1;315(5):1199-208. [Article]