Sulfite reductase [NADPH] hemoprotein beta-component (P17846)

Identification
Name:Sulfite reductase [NADPH] hemoprotein beta-component
Synonyms:
  • SiR-HP
  • SiRHP
Gene Name:cysI
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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
5.0Thumb+3.0Thumb+1.0Thumb ↔ 3.0Thumb+1.0Thumb+3.0Thumb
5.0Hydrogen ion + 3.0NADPH + 1.0Sulfite ↔ 3.0Water + 1.0Hydrogen sulfide + 3.0NADP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Flavin Mononucleotide + 1.0Hydrogen ion + 1.0NADPH ↔ 1.0FMNH + 1.0NADP
ReactionCard
1.0Thumb+3.0Thumb+3.0Thumb ↔ 1.0Thumb+3.0Thumb+3.0Thumb
1.0Hydrogen sulfide + 3.0NADP + 3.0Water ↔ 1.0Sulfite + 3.0NADPH + 3.0Hydrogen ion
ReactionCard
SMPDB Reactions:
3.0NADPH+5.0Thumb+1.0Sulfite+3.0Thumb+1.0Thumb → 1.0Thumb+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+3.0Thumb → 3.0Thumb+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+3.0Thumb → 1.0Sulfite+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+2.0Thumb → 1.0Riboflavin reduced+1.0Thumb
1.0Riboflavin + 1.0NADPH + 2.0Hydrogen ion → 1.0Riboflavin reduced + 1.0NADP
ReactionCard
EcoCyc Reactions:
5.0Thumb+3.0Thumb+1.0Thumb ↔ 3.0Thumb+1.0Thumb+3.0Thumb
5.0Hydrogen ion + 3.0NADPH + 1.0Sulfite ↔ 3.0Water + 1.0Hydrogen sulfide + 3.0NADP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0NADPH + 1.0Riboflavin → 1.0NADP + 1.0Reduced riboflavin
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Flavin Mononucleotide + 1.0Hydrogen ion + 1.0NADPH ↔ 1.0FMNH + 1.0NADP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0FAD + 1.0Hydrogen ion + 1.0NADPH → 1.0FADH2 + 1.0NADP
ReactionCard
1.0Thumb+3.0Thumb+3.0Thumb → 1.0Thumb+3.0Thumb
1.0Hydrogen sulfide + 3.0NADP + 3.0Water → 1.0Sulfite + 3.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB01520Flavin MononucleotideMetaboCard
ECMDB01142FMNHMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB21279Reduced riboflavinMetaboCard
ECMDB00244RiboflavinMetaboCard
ECMDB00598SulfideMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
macromolecular complex
protein complex
sulfite reductase complex (NADPH)
Function
4 iron, 4 sulfur cluster binding
binding
catalytic activity
cation binding
heme binding
ion binding
iron ion binding
iron-sulfur cluster binding
metal cluster binding
metal ion binding
NADP or NADPH 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 biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2763
Gene OrientationCounterclockwise
Centisome Percentage:62.21
Left Sequence End2886409
Right Sequence End2888121
Gene Sequence:
>1713 bp
ATGAGCGAAAAACATCCAGGGCCTTTAGTGGTCGAAGGAAAACTGACAGACGCCGAGCGC
ATGAAGCATGAAAGCAACTACCTGCGCGGCACCATTGCGGAAGATTTAAACGACGGTCTG
ACCGGCGGCTTTAAGGGCGACAACTTCCTGCTGATTCGCTTCCACGGCATGTATCAGCAG
GATGACCGCGACATCCGCGCCGAACGTGCTGAACAGAAGCTGGAGCCGCGCCACGCGATG
CTGCTTCGCTGTCGTCTGCCGGGTGGGGTGATTACCACTAAACAGTGGCAGGCGATCGAC
AAATTTGCCGGTGAAAACACCATCTATGGCAGCATTCGCCTGACCAACCGCCAGACGTTT
CAGTTCCACGGCATTCTGAAAAAGAACGTCAAACCGGTGCACCAGATGCTGCACTCGGTC
GGTCTTGATGCGCTGGCGACAGCTAACGACATGAACCGTAACGTACTCTGCACCTCGAAC
CCTTACGAGTCGCAGCTGCACGCGGAAGCGTACGAGTGGGCGAAGAAGATTTCTGAGCAT
CTGTTGCCTCGTACCCGCGCGTATGCGGAGATCTGGCTCGACCAGGAAAAAGTCGCCACT
ACTGATGAAGAACCGATCCTCGGCCAGACCTACCTGCCGCGTAAATTCAAAACCACGGTA
GTGATCCCGCCACAGAACGATATCGATCTGCACGCCAACGACATGAACTTCGTGGCGATC
GCCGAAAACGGCAAGCTGGTGGGCTTTAACCTGTTGGTGGGCGGTGGGCTTTCCATCGAA
CACGGCAACAAGAAAACCTACGCCCGCACCGCGAGTGAGTTTGGCTATCTGCCGCTGGAG
CATACGCTGGCGGTGGCCGAAGCCGTCGTGACAACTCAGCGTGACTGGGGTAACCGAACC
GATCGTAAAAATGCCAAAACCAAATACACGCTGGAGCGCGTGGGGGTTGAGACGTTTAAA
GCGGAAGTGGAGCGTCGCGCGGGGATCAAATTTGAACCGATCCGTCCATATGAGTTCACC
GGACGAGGCGATCGTATTGGCTGGGTTAAGGGCATTGATGATAACTGGCACCTGACGCTG
TTTATCGAAAATGGTCGCATCCTTGATTATCCGGCGCGTCCGCTGAAAACCGGCCTGCTG
GAGATCGCGAAGATCCACAAAGGCGATTTCCGCATTACGGCGAACCAGAATCTGATCATC
GCCGGTGTACCGGAAAGCGAGAAAGCGAAGATCGAGAAGATCGCCAAAGAGAGCGGGTTA
ATGAATGCCGTCACGCCGCAGCGTGAAAACTCGATGGCTTGCGTGTCATTCCCGACTTGC
CCGCTGGCGATGGCGGAAGCAGAGCGTTTCCTGCCGTCTTTTATCGACAACATCGATAAT
TTAATGGCGAAACATGGTGTCAGCGATGAGCATATCGTGATGCGTGTAACAGGCTGCCCG
AACGGTTGTGGTCGCGCGATGCTGGCGGAAGTGGGCCTGGTGGGTAAAGCGCCGGGTCGC
TACAACCTGCATCTTGGCGGCAACCGCATTGGGACACGTATCCCACGGATGTATAAAGAA
AACATCACCGAGCCGGAAATCCTGGCGTCGCTTGATGAACTGATAGGGCGCTGGGCGAAA
GAGCGCGAAGCGGGTGAAGGCTTCGGCGACTTTACGGTGCGTGCGGGCATCATTCGCCCG
GTGCTCGATCCGGCGCGTGATTTGTGGGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:570
Protein Molecular Weight:63998
Protein Theoretical pI:8
PDB File:8GEP
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Sulfite reductase [NADPH] hemoprotein beta-component
MSEKHPGPLVVEGKLTDAERMKHESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQ
DDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTF
QFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKISEH
LLPRTRAYAEIWLDQEKVATTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAI
AENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRT
DRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTL
FIENGRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGL
MNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGCP
NGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAK
EREAGEGFGDFTVRAGIIRPVLDPARDLWD
References
External Links:
ResourceLink
Uniprot ID:P17846
Uniprot Name:CYSI_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675584
PDB ID:8GEP
Ecogene ID:EG10190
Ecocyc:EG10190
ColiBase:b2763
Kegg Gene:b2763
EchoBASE ID:EB0187
CCDB:CYSI_ECOLI
BacMap:16130670
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
  • Crane, B. R., Siegel, L. M., Getzoff, E. D. (1995). "Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions." Science 270:59-67. Pubmed: 7569952
  • Crane, B. R., Siegel, L. M., Getzoff, E. D. (1997). "Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange." Biochemistry 36:12101-12119. Pubmed: 9315848
  • 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
  • Krone, F. A., Westphal, G., Schwenn, J. D. (1991). "Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli." Mol Gen Genet 225:314-319. Pubmed: 2005873
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • 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