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
- Functions4 iron, 4 sulfur cluster binding / heme binding / metal ion binding / NADP binding / 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.
- 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
Resource Link UniProtKB ID P17846 UniProtKB Entry Name CYSI_ECOLI GenBank Protein ID 145680 GenBank Gene ID M23008 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]