Cytochrome c-552

Details

Name
Cytochrome c-552
Synonyms
  • 1.7.2.2
  • Ammonia-forming cytochrome c nitrite reductase
  • Cytochrome c nitrite reductase
Gene Name
nrfA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011463|Cytochrome c-552
MTRIKINARRIFSLLIPFFFFTSVHAEQTAAPAKPVTVEAKNETFAPQHPDQYLSWKATS
EQSERVDALAEDPRLVILWAGYPFSRDYNKPRGHAFAVTDVRETLRTGAPKNAEDGPLPM
ACWSCKSPDVARLIQKDGEDGYFHGKWARGGPEIVNNLGCADCHNTASPEFAKGKPELTL
SRPYAARAMEAIGKPFEKAGRFDQQSMVCGQCHVEYYFDGKNKAVKFPWDDGMKVENMEQ
YYDKIAFSDWTNSLSKTPMLKAQHPEYETWTAGIHGKNNVTCIDCHMPKVQNAEGKLYTD
HKIGNPFDNFAQTCANCHTQDKAALQKVVAERKQSINDLKIKVEDQLVHAHFEAKAALDA
GATEAEMKPIQDDIRHAQWRWDLAIASHGIHMHAPEEGLRMLGTAMDKAADARTKLARLL
ATKGITHEIQIPDISTKEKAQQAIGLNMEQIKAEKQDFIKTVIPQWEEQARKNGLLSQ
Number of residues
478
Molecular Weight
53702.545
Theoretical pI
7.27
GO Classification
Functions
calcium ion binding / heme binding / iron ion binding / nitric oxide reductase activity / nitrite reductase (cytochrome, ammonia-forming) activity
Processes
anaerobic electron transport chain / nitrate assimilation
Components
outer membrane-bounded periplasmic space
General Function
Nitrite reductase (cytochrome, ammonia-forming) activity
Specific Function
Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:9593308, PubMed:11863430, PubMed:18311941, PubMed:20629638). Has very low activity toward hydroxylamine (PubMed:11863430). Has even lower activity toward sulfite (PubMed:20629638). Sulfite reductase activity is maximal at neutral pH (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0011464|Cytochrome c-552 (nrfA)
ATGACAAGGATAAAAATAAACGCACGCCGTATCTTCAGCTTATTGATTCCTTTTTTCTTT
TTCACTTCTGTTCACGCTGAACAAACGGCTGCTCCCGCAAAACCTGTAACTGTGGAAGCG
AAGAATGAAACCTTTGCCCCGCAGCATCCCGATCAATATCTCTCCTGGAAAGCCACCTCG
GAACAGTCAGAGCGTGTTGACGCCCTGGCGGAAGATCCACGGCTGGTGATCCTGTGGGCG
GGGTATCCCTTCTCGCGCGATTACAACAAGCCGCGTGGACATGCTTTTGCTGTGACCGAT
GTGCGTGAAACCCTGCGTACCGGTGCGCCGAAAAACGCTGAAGATGGTCCGCTACCGATG
GCATGCTGGAGTTGTAAAAGCCCGGATGTGGCGCGTCTGATCCAGAAAGACGGCGAAGAT
GGCTACTTCCACGGTAAATGGGCGCGCGGCGGTCCGGAAATCGTCAACAACTTAGGTTGT
GCCGATTGCCATAACACCGCCTCTCCAGAGTTCGCCAAAGGCAAACCGGAGTTAACCCTT
TCCCGTCCGTATGCGGCTCGCGCGATGGAAGCCATTGGTAAACCTTTTGAGAAAGCCGGA
CGTTTCGACCAGCAATCGATGGTTTGCGGTCAGTGCCATGTGGAGTATTACTTCGACGGC
AAAAACAAAGCGGTTAAATTCCCGTGGGATGACGGCATGAAAGTCGAAAATATGGAGCAG
TATTACGACAAAATTGCCTTCTCTGACTGGACTAACTCCCTGTCGAAAACGCCAATGCTG
AAAGCGCAGCACCCGGAATATGAAACCTGGACAGCGGGCATTCACGGTAAAAACAACGTG
ACCTGTATCGACTGCCATATGCCAAAAGTGCAGAACGCCGAAGGCAAACTCTACACCGAC
CATAAAATTGGTAATCCGTTTGATAACTTCGCCCAGACTTGTGCGAACTGCCATACCCAG
GACAAAGCTGCCTTGCAAAAAGTGGTCGCGGAACGTAAGCAGTCGATTAACGACCTGAAA
ATCAAGGTTGAAGATCAACTGGTTCACGCTCACTTCGAAGCGAAAGCAGCGCTGGATGCA
GGCGCGACGGAAGCTGAAATGAAGCCAATTCAGGACGATATCCGTCATGCCCAGTGGCGC
TGGGATCTGGCGATCGCTTCCCACGGCATTCATATGCACGCACCGGAAGAAGGTTTACGG
ATGCTCGGTACGGCGATGGATAAAGCGGCGGATGCACGCACCAAACTGGCGCGCCTGCTG
GCGACCAAAGGCATCACCCATGAAATCCAGATCCCGGATATCTCAACCAAAGAGAAAGCC
CAGCAGGCCATTGGCCTGAACATGGAACAAATCAAGGCCGAGAAGCAGGACTTCATCAAA
ACGGTGATCCCGCAGTGGGAAGAACAGGCACGTAAAAACGGTCTGTTAAGCCAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0ABK9
UniProtKB Entry NameNRFA_ECOLI
GenBank Protein ID853826
GenBank Gene IDX72298
General References
  1. Darwin A, Hussain H, Griffiths L, Grove J, Sambongi Y, Busby S, Cole J: Regulation and sequence of the structural gene for cytochrome c552 from Escherichia coli: not a hexahaem but a 50 kDa tetrahaem nitrite reductase. Mol Microbiol. 1993 Sep;9(6):1255-65. [Article]
  2. Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [Article]
  3. 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]
  4. 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]
  5. Iobbi-Nivol C, Crooke H, Griffiths L, Grove J, Hussain H, Pommier J, Mejean V, Cole JA: A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12. FEMS Microbiol Lett. 1994 Jun 1;119(1-2):89-94. [Article]
  6. Eaves DJ, Grove J, Staudenmann W, James P, Poole RK, White SA, Griffiths I, Cole JA: Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli. Mol Microbiol. 1998 Apr;28(1):205-16. [Article]
  7. Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ: Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli. Biochemistry. 2002 Mar 5;41(9):2921-31. [Article]
  8. Clarke TA, Kemp GL, Van Wonderen JH, Doyle RM, Cole JA, Tovell N, Cheesman MR, Butt JN, Richardson DJ, Hemmings AM: Role of a conserved glutamine residue in tuning the catalytic activity of Escherichia coli cytochrome c nitrite reductase. Biochemistry. 2008 Mar 25;47(12):3789-99. doi: 10.1021/bi702175w. Epub 2008 Mar 1. [Article]
  9. Kemp GL, Clarke TA, Marritt SJ, Lockwood C, Poock SR, Hemmings AM, Richardson DJ, Cheesman MR, Butt JN: Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coli. Biochem J. 2010 Oct 1;431(1):73-80. doi: 10.1042/BJ20100866. [Article]
  10. Lockwood CW, Clarke TA, Butt JN, Hemmings AM, Richardson DJ: Characterization of the active site and calcium binding in cytochrome c nitrite reductases. Biochem Soc Trans. 2011 Dec;39(6):1871-5. doi: 10.1042/BST20110731. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03317Ferroheme CexperimentalunknownDetails