Sulfite reductase [NADPH] hemoprotein beta-component

Details

Name
Sulfite reductase [NADPH] hemoprotein beta-component
Synonyms
  • 1.8.1.2
  • SiR-HP
Gene Name
cysI
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0003764|Sulfite reductase [NADPH] hemoprotein beta-component
MSEKHPGPLVVEGKLTDAERMKHESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQ
DDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTF
QFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKISEH
LLPRTRAYAEIWLDQEKVATTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAI
AENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRT
DRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTL
FIENGRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGL
MNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGCP
NGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAK
EREAGEGFGDFTVRAGIIRPVLDPARDLWD
Number of residues
570
Molecular Weight
63997.615
Theoretical pI
7.7
GO Classification
Functions
4 iron, 4 sulfur cluster binding / heme binding / metal ion binding / NADP binding / 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011362|Sulfite reductase [NADPH] hemoprotein beta-component (cysI)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP17846
UniProtKB Entry NameCYSI_ECOLI
GenBank Protein ID145680
GenBank Gene IDM23008
General References
  1. 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]
  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. [Article]
  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. [Article]
  4. Krone FA, Westphal G, Schwenn JD: Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli. Mol Gen Genet. 1991 Feb;225(2):314-9. [Article]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  6. Crane BR, Siegel LM, Getzoff ED: Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Science. 1995 Oct 6;270(5233):59-67. [Article]
  7. Crane BR, Siegel LM, Getzoff ED: 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. 1997 Oct 7;36(40):12101-19. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02832SirohemeexperimentalunknownDetails