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
- Functionselectron carrier activity / heme binding / hydroxylamine reductase activity / metal ion binding / nitrite reductase (NO-forming) activityComponentsperiplasmic space
- General Function
- Nitrite reductase (no-forming) activity
- Specific Function
- Not Available
- Pfam Domain Function
- Cytochrome_CBB3 (PF13442)
- 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
Resource Link UniProtKB ID P72181 UniProtKB Entry Name NIRS_PARPN GenBank Protein ID 1654415 GenBank Gene ID U75413 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]