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
- Functionsflavin 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) activityProcessescysteine biosynthetic process / hydrogen sulfide biosynthetic process / sulfate assimilationComponentssulfite 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
Resource Link UniProtKB ID P38038 UniProtKB Entry Name CYSJ_ECOLI GenBank Gene ID M23008 - General References
- 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. [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]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]