Nitrite reductase

Details

Name
Nitrite reductase
Synonyms
  • 1.7.2.1
  • Cytochrome cd1
  • Cytochrome oxidase
  • Hydroxylamine reductase
Gene Name
nirS
Organism
Paracoccus pantotrophus
Amino acid sequence
>lcl|BSEQ0011288|Nitrite reductase
MRQRTPFARPGLLASAALALVLGPLAASAQEQVAPPKDPAAALEDHKTRTDNRYEPSLDN
LAQQDVAAPGAPEGVSALSDAQYNEANKIYFERCAGCHGVLRKGATGKALTPDLTRDLGF
DYLQSFITYGSPAGMPNWGTSGELSAEQVDLMANYLLLDPAAPPEFGMKEMRESWKVHVA
PEDRPTQQENDWDLENLFSVTLRDAGQIALIDGATYEIKSVLDTGYAVHISRLSASGRYL
FVIGRDGKVNMIDLWMKEPTTVAEIKIGSEARSIETSKMEGWEDKYAIAGAYWPPQYVIM
DGETLEPKKIQSTRGMTYDEQEYHPEPRVAAILASHYRPEFIVNVKETGKILLVDYTDLD
NLKTTEISAERFLHDGGLDGSHRYFITAANARNKLVVIDTKEGKLVAIEDTGGQTPHPGR
GANFVHPTFGPVWATSHMGDDSVALIGTDPEGHPDNAWKILDSFPALGGGSLFIKTHPNS
QYLYVDATLNPEAEISGSVAVFDIKAMTGDGSDPEFKTLPIAEWAGITEGQPRVVQGEFN
KDGTEVWFSVWNGKDQESALVVVDDKTLELKHVIKDERLVTPTGKFNVYNTMTDTY
Number of residues
596
Molecular Weight
65382.815
Theoretical pI
4.59
GO Classification
Functions
electron carrier activity / heme binding / hydroxylamine reductase activity / metal ion binding / nitrite reductase (NO-forming) activity
Components
periplasmic space
General Function
Nitrite reductase (no-forming) activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0003571|1791 bp
ATGAGACAAAGGACTCCATTCGCCAGACCCGGCCTCCTGGCCTCGGCAGCCCTGGCCCTT
GTCCTTGGACCGCTTGCGGCCGCGGCACAGGAACAGGTCGCCCCGCCAAAGGATCCAGCC
GCCGCGCTGGAGGACCACAAGACGCGCACCGACAATCGCTATGAGCCCTCGCTGGACAAC
CTTGCGCAGCAGGATGTCGCGGCTCCCGGGGCCCCCGAGGGTGTCACGGCCCTGTCCGAT
GCCCAATACAACGAGGCCAACAAGATCTATTTCGAACGCTGCGCCGGCTGCCACGGCGTG
TTGCGCAAAGGCGCGACCGGCAAGGCGCTGACCCCTGACCTGACCCGCGATCTGGGCTTT
GACTACCTGCAAAGCTTCATCACCTACGCCTCGCCGGCGGGGATGCCGAACTGGGGCACC
TCGGGCGAGTTGTCGGCCGAGCAGGTCGACCTGATGGCCAACTACCTGCTTCTGGACCCG
GCCGCGCCGCCGGAATTCGGCATGAAGGAGATGCGCGAATCCTGGAAGGTGCATGTCGCG
CCGGAAGACCGGCCGACCCAGCAGGAAAACGACTGGGATCTGGAAAACCTGTTCAGCGTC
ACCCTGCGCGACGCCGGCCAGATCGCGCTGATCGACGGCACCACCTATGAGATCAAGTCG
GTCCTCGACACCGGCTATGCGGTCCATATCAGCCGGCTGTCCGCATCGGGCCGCTACCTG
TTCGTGATCGGCCGCGACGGCAAGGTCAACATGATCGACCTGTGGATGAAGGAGCCCACC
ACCGTTGCCGAGATCAAGATCGGCTCGGAGGCGCGTTCCATCGAGACCTCGAAGATGGAG
GGCTGGGAGGACAAATACGCCATCGCCGGGGCCTATTGGCCGCCGCAATACGTCATCATG
GACGGCGAGACGCTGGAGCCGAAAAAGATCCAGTCCACGCGCGGCATGACCTATGACGAG
CAGGAATATCACCCCGAGCCGCGCGTCGCCGCGATCCTCGCCAGCCATTACCGGCCCGAG
TTCATCGTGAACGTCAAGGAAACGGGCAAGATCCTGCTGGTCGACTATACCGACCTCGAC
AACCTCAAGACCACCGAGATCAGCGCCGAACGCTTCCTGCACGACGGCGGCCTGGACGGC
TCGCACCGCTATTTCATCACCGCGGCGAACGCCCGCAACAAGCTGGTGGTGATCGACACC
AAGGAAGGCAAGCTGGTCGCGATCGAGGATACCGGCGGCCAGACCCCGCATCCGGGCCGC
GGCGCGAACTTCGTCCACCCGACCTTCGGGCCGGTCTGGGCGACCTCGCATATGGGCGAC
GATTCGGTGGCGCTGATCGGCACCGATCCCGAGGGCCATCCCGACAATGCCTGGAAGATC
CTCGACAGCTTCCCGGCGTTGGGGGGCGGCTCGCTGTTCATCAAGACGCACCCGAACTCG
CAATATCTCTATGTCGATGCGACCCTGAACCCCGAGGCCGAGATTTCCGGCTCGGTCGCG
GTGTTCGACATCAAGGCGATGACGGGCGACGGTTCGGACCCCGAGTTCAAGACCCTGCCC
ATCGCCGAATGGGCCGGCATCACCGAAGGCCAGCCCCGCGTCGTGCAGGGCGAGTTCAAC
AAGGACGGCACCGAGGTCTGGTTCAGCGTCTGGAACGGCAAGGACCAGGAATCGGCGCTG
GTCGTGGTGGACGACAAGACGCTGGAACTTAAGCACGTCATCAAGGACGAGCGGCTGGTG
ACGCCCACCGGCAAGTTCAACGTCTACAACACCATGACCGACACCTATTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP72181
UniProtKB Entry NameNIRS_PARPN
GenBank Protein ID1654415
GenBank Gene IDU75413
General References
  1. Saunders NF, Ferguson SJ, Baker SC: Transcriptional analysis of the nirS gene, encoding cytochrome cd1 nitrite reductase, of Paracoccus pantotrophus LMD 92.63. Microbiology. 2000 Feb;146 ( Pt 2):509-16. [PubMed:10708389]
  2. Gordon EH, Steensma E, Ferguson SJ: The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli. Biochem Biophys Res Commun. 2001 Mar 2;281(3):788-94. [PubMed:11237728]
  3. Fulop V, Moir JW, Ferguson SJ, Hajdu J: The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1. Cell. 1995 May 5;81(3):369-77. [PubMed:7736589]
  4. Baker SC, Saunders NF, Willis AC, Ferguson SJ, Hajdu J, Fulop V: Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds. J Mol Biol. 1997 Jun 13;269(3):440-55. [PubMed:9199411]
  5. Williams PA, Fulop V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J: Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature. 1997 Sep 25;389(6649):406-12. [PubMed:9311786]
  6. Sjogren T, Svensson-Ek M, Hajdu J, Brzezinski P: Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study. Biochemistry. 2000 Sep 12;39(36):10967-74. [PubMed:10998233]
  7. Jafferji A, Allen JW, Ferguson SJ, Fulop V: X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus. J Biol Chem. 2000 Aug 18;275(33):25089-94. [PubMed:10827177]
  8. Sjogren T, Hajdu J: Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase. J Biol Chem. 2001 Apr 20;276(16):13072-6. Epub 2001 Jan 26. [PubMed:11278884]
  9. Sjogren T, Hajdu J: The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase. J Biol Chem. 2001 Aug 3;276(31):29450-5. Epub 2001 May 23. [PubMed:11373294]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03309N-cyclohexyltaurineexperimentalunknownDetails
DB03317Heme CexperimentalunknownDetails
DB03469Heme DexperimentalunknownDetails