Identification
Name:Sulfite reductase [NADPH] flavoprotein alpha-component
Synonyms:
  • SiR-FP
Gene Name:cysJ
Enzyme Class:
Biological Properties
General Function:Involved in sulfite reductase (NADPH) activity
Specific Function:Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L- cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
5.0Thumb+3.0Thumb+1.0Thumb3.0Thumb+1.0Thumb+3.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+3.0Thumb+3.0Thumb1.0Thumb+3.0Thumb+3.0Thumb
SMPDB Reactions:
3.0NADPH+5.0Thumb+1.0Sulfite+3.0Thumb+1.0Thumb1.0Thumb+3.0Thumb+3.0Thumb
3.0NADPH + 5.0Hydrogen ion + 1.0Sulfite + 3.0NADPH + 1.0Sulfite → 1.0Hydrogen sulfide + 3.0Water + 3.0NADP
ReactionCard
1.0Sulfite+3.0NADPH+5.0Thumb+1.0Thumb+3.0Thumb3.0Thumb+1.0Thumb+1.0Thumb
1.0Sulfite + 3.0NADPH + 5.0Hydrogen ion + 1.0Sulfite + 3.0NADPH → 3.0Water + 1.0NADP + 1.0Hydrogen sulfide
ReactionCard
1.0Thumb+1.0Thumb+3.0Thumb1.0Sulfite+3.0NADPH+1.0Thumb+3.0Thumb
1.0Sulfide + 1.0Water + 3.0NADP → 1.0Sulfite + 3.0NADPH + 1.0Sulfite + 3.0NADPH
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb1.0Riboflavin reduced+1.0Thumb
1.0Riboflavin + 1.0NADPH + 2.0Hydrogen ion → 1.0Riboflavin reduced + 1.0NADP
ReactionCard
EcoCyc Reactions:
5.0Thumb+3.0Thumb+1.0Thumb3.0Thumb+1.0Thumb+3.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0FAD + 1.0Hydrogen ion + 1.0NADPH → 1.0FADH2 + 1.0NADP
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB01520Flavin MononucleotideMetaboCard
ECMDB01142FMNHMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB21279Reduced riboflavinMetaboCard
ECMDB00244RiboflavinMetaboCard
ECMDB00598SulfideMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
FMN binding
ion binding
iron ion binding
metal ion binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
oxidoreductase activity, acting on NADH or NADPH
sulfite reductase (NADPH) activity
transition metal ion binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
cysteine biosynthetic process
metabolic process
oxidation reduction
sulfate assimilation
sulfur amino acid biosynthetic process
sulfur amino acid metabolic process
sulfur metabolic process
Gene Properties
Blattner:b2764
Gene OrientationCounterclockwise
Centisome Percentage:62.25
Left Sequence End2888121
Right Sequence End2889920
Gene Sequence:
>1800 bp
ATGACGACACAGGTCCCACCTTCCGCGTTGCTTCCGTTGAACCCGGAGCAACTGGCACGC
CTTCAGGCGGCCACGACCGATTTAACTCCCACCCAGCTTGCCTGGGTTTCTGGCTATTTC
TGGGGCGTACTCAATCAGCAGCCTGCTGCGCTTGCAGCGACGCCAGCGCCAGCCGCAGAA
ATGCCGGGTATAACTATTATCTCCGCCTCGCAAACCGGCAATGCGCGCCGGGTTGCTGAA
GCATTACGTGATGATTTATTAGCAGCAAAACTGAACGTTAAGCTGGTGAACGCGGGCGAC
TATAAATTCAAACAAATCGCCAGCGAAAAACTGCTCATCGTAGTGACGTCAACGCAAGGG
GAAGGGGAACCGCCGGAAGAAGCCGTCGCGCTGCATAAGTTCCTGTTCTCCAAAAAAGCG
CCAAAGCTGGAAAACACCGCGTTTGCCGTGTTTAGCCTCGGCGATAGCTCTTATGAATTT
TTCTGCCAGTCCGGGAAAGATTTCGACAGCAAGCTGGCGGAACTGGGTGGTGAACGCCTG
CTCGACCGTGTCGATGCCGATGTTGAATACCAGGCTGCTGCCAGCGAGTGGCGCGCCCGC
GTGGTTGATGCGCTTAAATCGCGTGCGCCTGTCGCGGCACCTTCGCAATCCGTCGCTACT
GGCGCGGTAAATGAAATCCACACCAGCCCGTACAGCAAAGACGCGCCGCTGGTGGCTAGC
CTCTCTGTTAACCAGAAAATTACCGGGCGTAACTCTGAAAAAGACGTTCGCCATATCGAA
ATTGACTTAGGTGACTCGGGCATGCGTTACCAGCCGGGTGACGCGCTGGGCGTCTGGTAT
CAGAACGATCCGGCACTGGTGAAAGAACTTGTCGAACTGCTGTGGCTGAAAGGCGATGAA
CCTGTCACCGTCGAGGGCAAAACGTTGCCTCTGAACGAAGCGCTACAGTGGCACTTCGAA
CTGACCGTCAACACCGCCAACATTGTTGAGAATTACGCCACGCTTACCCGCAGTGAAACA
CTGCTGCCGCTGGTGGGCGATAAAGCGAAGTTACAGCATTACGCCGCGACGACGCCGATT
GTTGACATGGTGCGTTTCTCCCCGGCACAGCTTGATGCCGAAGCGCTAATTAATCTGCTG
CGCCCGCTGACGCCGCGTCTGTATTCCATCGCCTCCTCGCAGGCGGAAGTCGAGAACGAA
GTACACGTCACCGTTGGTGTGGTGCGTTACGACGTGGAAGGCCGCGCCCGTGCCGGTGGT
GCCTCCAGCTTCCTCGCTGACCGCGTGGAAGAAGAGGGCGAAGTCCGCGTATTTATCGAA
CATAACGATAACTTCCGCCTGCCAGCCAATCCAGAAACCCCGGTGATTATGATTGGCCCA
GGCACCGGTATTGCGCCGTTCCGCGCCTTTATGCAGCAACGCGCCGCCGACGAAGCGCCA
GGTAAAAACTGGCTGTTCTTTGGTAATCCGCACTTTACGGAAGACTTCCTGTACCAGGTG
GAGTGGCAGCGCTACGTCAAAGATGGCGTGCTGACACGTATCGATCTTGCCTGGTCGCGC
GATCAAAAAGAAAAAGTTTACGTACAAGACAAACTGCGCGAACAGGGCGCGGAGCTGTGG
CGCTGGATCAATGATGGTGCCCACATTTATGTCTGCGGCGACGCTAATCGCATGGCGAAA
GACGTTGAGCAGGCACTTCTGGAAGTGATTGCCGAATTTGGTGGCATGGACACCGAAGCG
GCGGATGAATTTTTAAGTGAGCTGCGCGTAGAGCGCCGTTATCAGCGAGATGTCTACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:599
Protein Molecular Weight:66269
Protein Theoretical pI:5
PDB File:1DDI
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Sulfite reductase [NADPH] flavoprotein alpha-component
MTTQVPPSALLPLNPEQLARLQAATTDLTPTQLAWVSGYFWGVLNQQPAALAATPAPAAE
MPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQG
EGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDSSYEFFCQSGKDFDSKLAELGGERL
LDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVAS
LSVNQKITGRNSEKDVRHIEIDLGDSGMRYQPGDALGVWYQNDPALVKELVELLWLKGDE
PVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPI
VDMVRFSPAQLDAEALINLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGG
ASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAP
GKNWLFFGNPHFTEDFLYQVEWQRYVKDGVLTRIDLAWSRDQKEKVYVQDKLREQGAELW
RWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY
References
External Links:
ResourceLink
Uniprot ID:P38038
Uniprot Name:CYSJ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675585
PDB ID:1DDI
Ecogene ID:EG10191
Ecocyc:EG10191
ColiBase:b2764
Kegg Gene:b2764
EchoBASE ID:EB0188
CCDB:CYSJ_ECOLI
BacMap:16130671
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
  • Champier, L., Sibille, N., Bersch, B., Brutscher, B., Blackledge, M., Coves, J. (2002). "Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain." Biochemistry 41:3770-3780. Pubmed: 11888295
  • Coves, J., Lebrun, C., Gervasi, G., Dalbon, P., Fontecave, M. (1999). "Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride." Biochem J 342 ( Pt 2):465-472. Pubmed: 10455035
  • Coves, J., Zeghouf, M., Macherel, D., Guigliarelli, B., Asso, M., Fontecave, M. (1997). "Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli." Biochemistry 36:5921-5928. Pubmed: 9153434
  • Eschenbrenner, M., Coves, J., Fontecave, M. (1995). "NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction." FEBS Lett 374:82-84. Pubmed: 7589518
  • Eschenbrenner, M., Coves, J., Fontecave, M. (1995). "The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure." J Biol Chem 270:20550-20555. Pubmed: 7657631
  • Gruez, A., Pignol, D., Zeghouf, M., Coves, J., Fontecave, M., Ferrer, J. L., Fontecilla-Camps, J. C. (2000). "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol 299:199-212. Pubmed: 10860732
  • 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
  • Ostrowski, J., Barber, M. J., Rueger, D. C., Miller, B. E., Siegel, L. M., Kredich, N. M. (1989). "Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase." J Biol Chem 264:15796-15808. Pubmed: 2550423
  • Ostrowski, J., Wu, J. Y., Rueger, D. C., Miller, B. E., Siegel, L. M., Kredich, N. M. (1989). "Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase." J Biol Chem 264:15726-15737. Pubmed: 2670946
  • Sibille, N., Blackledge, M., Brutscher, B., Coves, J., Bersch, B. (2005). "Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli." Biochemistry 44:9086-9095. Pubmed: 15966732
  • Zeghouf, M., Defaye, G., Fontecave, M., Coves, J. (1998). "The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase." Biochem Biophys Res Commun 246:602-605. Pubmed: 9618257
  • Zeghouf, M., Fontecave, M., Coves, J. (2000). "A simplifed functional version of the Escherichia coli sulfite reductase." J Biol Chem 275:37651-37656. Pubmed: 10984484
  • Zeghouf, M., Fontecave, M., Macherel, D., Coves, J. (1998). "The flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors." Biochemistry 37:6114-6123. Pubmed: 9558350