Sulfite reductase [NADPH] flavoprotein alpha-component

Details

Name
Sulfite reductase [NADPH] flavoprotein alpha-component
Synonyms
  • 1.8.1.2
  • SiR-FP
Gene Name
cysJ
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020642|Sulfite reductase [NADPH] flavoprotein alpha-component
MTTQVPPSALLPLNPEQLARLQAATTDLTPTQLAWVSGYFWGVLNQQPAALAATPAPAAE
MPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQG
EGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDSSYEFFCQSGKDFDSKLAELGGERL
LDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVAS
LSVNQKITGRNSEKDVRHIEIDLGDSGMRYQPGDALGVWYQNDPALVKELVELLWLKGDE
PVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPI
VDMVRFSPAQLDAEALINLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGG
ASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAP
GKNWLFFGNPHFTEDFLYQVEWQRYVKDGVLTRIDLAWSRDQKEKVYVQDKLREQGAELW
RWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY
Number of residues
599
Molecular Weight
66269.23
Theoretical pI
4.66
GO Classification
Functions
flavin adenine dinucleotide binding / FMN binding / iron ion binding / NADPH-hemoprotein reductase activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen / riboflavin reductase (NADPH) activity / sulfite reductase (NADPH) activity
Processes
cysteine biosynthetic process / hydrogen sulfide biosynthetic process / sulfate assimilation
Components
sulfite reductase complex (NADPH)
General Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0020643|Sulfite reductase [NADPH] flavoprotein alpha-component (cysJ)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP38038
UniProtKB Entry NameCYSJ_ECOLI
GenBank Gene IDM23008
General References
  1. Ostrowski J, Barber MJ, Rueger DC, Miller BE, Siegel LM, Kredich NM: 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. 1989 Sep 25;264(27):15796-808. [PubMed:2550423]
  2. 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. [PubMed:9278503]
  3. 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. [PubMed:16738553]
  4. Ostrowski J, Wu JY, Rueger DC, Miller BE, Siegel LM, Kredich NM: 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. 1989 Sep 15;264(26):15726-37. [PubMed:2670946]
  5. Eschenbrenner M, Coves J, Fontecave M: NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction. FEBS Lett. 1995 Oct 23;374(1):82-4. [PubMed:7589518]
  6. Eschenbrenner M, Coves J, Fontecave M: The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. J Biol Chem. 1995 Sep 1;270(35):20550-5. [PubMed:7657631]
  7. Coves J, Zeghouf M, Macherel D, Guigliarelli B, Asso M, Fontecave M: Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. Biochemistry. 1997 May 13;36(19):5921-8. [PubMed:9153434]
  8. Zeghouf M, Defaye G, Fontecave M, Coves J: The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase. Biochem Biophys Res Commun. 1998 May 29;246(3):602-5. [PubMed:9618257]
  9. Zeghouf M, Fontecave M, Macherel D, Coves J: 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. 1998 Apr 28;37(17):6114-23. [PubMed:9558350]
  10. Coves J, Lebrun C, Gervasi G, Dalbon P, Fontecave M: Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride. Biochem J. 1999 Sep 1;342 ( Pt 2):465-72. [PubMed:10455035]
  11. Champier L, Sibille N, Bersch B, Brutscher B, Blackledge M, Coves J: Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain. Biochemistry. 2002 Mar 19;41(11):3770-80. [PubMed:11888295]
  12. Zeghouf M, Fontecave M, Coves J: A simplifed functional version of the Escherichia coli sulfite reductase. J Biol Chem. 2000 Dec 1;275(48):37651-6. [PubMed:10984484]
  13. Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC: Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. J Mol Biol. 2000 May 26;299(1):199-212. [PubMed:10860732]
  14. Sibille N, Blackledge M, Brutscher B, Coves J, Bersch B: Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli. Biochemistry. 2005 Jun 28;44(25):9086-95. [PubMed:15966732]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails
DB03461Nicotinamide adenine dinucleotide phosphateexperimentalunknownDetails