Copper-containing nitrite reductase

Details

Name
Copper-containing nitrite reductase
Synonyms
  • Dissimilatory copper-containing nitrite reductase
  • nirK
  • Nitrite Reductase (NiR)
Gene Name
nir
Organism
Alcaligenes xylosoxydans xylosoxydans
Amino acid sequence
>lcl|BSEQ0022433|Copper-containing nitrite reductase
MNALRPTLLAAALAFTMAAGTAWAQDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFT
MTIEEKKMVIDDKGTTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGA
TGALGGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVLPRDGL
KDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTVQVMRTLTPSHIVFNG
KVGALTGANALTAKVGETVLLIHSQANRDTRPHLIGGHGDWVWETGKFANPPQRDLETWF
IRGGSAGAALYTFKQPGVYAYLNHNLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR
Number of residues
360
Molecular Weight
38939.295
Theoretical pI
7.55
GO Classification
Functions
copper ion binding / nitrite reductase (NO-forming) activity
Processes
nitrogen compound metabolic process
General Function
Nitrite reductase (no-forming) activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0005488|1083 bp
ATGAACGCATTACGGCCCACTTTGCTGGCGGCGGCGCTGGCTTTTACGATGGCCGCCGGG
ACCGCCTGGGCGCAGGACGCCGACAAGCTGCCCCATACCAAGGTCACGCTGGTCGCTCCG
CCCCAGGTGCATCCGCACGAGCAGGCGACCAAGTCGGGCCCCAAAGTCGTCGAATTCACC
ATGACCATCGAGGAAAAGAAGATGGTGATCGACGACAAGGGCACGACGCTGCAGGCCATG
ACGTTCAACGGCTCCATGCCCGGCCCCACGCTGGTGGTGCACGAGGGCGACTACGTCCAG
CTGACGCTGGTCAACCCGGCCACCAACGCCATGCCGCACAACGTCGACTTCCACGGCGCC
ACCGGCGCGCTGGGCGGCGCCAAGCTCACCAACGTCAACCCTGGCGAGCAGGCTACGCTG
CGCTTCAAGGCCGACCGCAGCGGCACCTTCGTCTACCACTGCGCGCCCGAAGGCATGGTG
CCCTGGCACGTGGTGTCGGGCATGAGCGGCACGCTGATGGTGCTGCCGCGCGACGGCCTG
AAGGATCCGCAGGGCAAGCCGCTGCATTACGACCGCGCCTACACCATCGGCGAGTTCGAC
CTGTACATCCCCAAGGGCCCGGACGGCAAGTACAAGGACTACGCCACGCTGGCCGAAAGC
TATGGCGACACGGTGCAGGTGATGCGCACGCTGACGCCGTCGCACATCGTCTTCAATGGC
AAGGTCGGCGCGCTGACCGGCGCCAACGCGCTCACCGCCAAGGTCGGCGAGACCGTGCTG
CTGATCCACTCGCAGGCCAATCGCGACACCCGCCCGCACCTGATCGGCGGCCATGGCGAC
TGGGTCTGGGAGACCGGCAAGTTCGCCAACCCGCCGCAGCGCGACCTGGAAACCTGGTTC
ATCCGCGGCGGGTCGGCCGGCGCCGCGCTCTACACCTTCAAGCAGCCTGGCGTGTATGCC
TACCTGAACCACAACCTGATCGAGGCCTTCGAACTGGGCGCGGCCGGCCACATCAAGGTC
GAGGGCAAGTGGAACGACGACCTGATGAAGCAGATCAAGGCGCCCGCGCCGATTCCGCGC
TGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO68601
UniProtKB Entry NameO68601_ALCXX
GenBank Gene IDAF051831
General References
  1. Inoue T, Gotowda M, Deligeer, Kataoka K, Yamaguchi K, Suzuki S, Watanabe H, Gohow M, Kai Y: Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 A resolution: comparison of blue and green nitrite reductases. J Biochem. 1998 Nov;124(5):876-9. [Article]
  2. Dodd FE, Van Beeumen J, Eady RR, Hasnain SS: X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner. J Mol Biol. 1998 Sep 18;282(2):369-82. [Article]
  3. Ellis MJ, Dodd FE, Strange RW, Prudencio M, Sawers G, Eady RR, Hasnain SS: X-ray structure of a blue copper nitrite reductase at high pH and in copper-free form at 1.9 A resolution. Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1110-8. Epub 2001 Jul 23. [Article]
  4. Ellis MJ, Prudencio M, Dodd FE, Strange RW, Sawers G, Eady RR, Hasnain SS: Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism. J Mol Biol. 2002 Feb 8;316(1):51-64. [Article]
  5. Ellis MJ, Dodd FE, Sawers G, Eady RR, Hasnain SS: Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu. J Mol Biol. 2003 Apr 25;328(2):429-38. [Article]
  6. Barrett ML, Harris RL, Antonyuk S, Hough MA, Ellis MJ, Sawers G, Eady RR, Hasnain SS: Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: crystal structures of the Trp138His and His313Gln mutants. Biochemistry. 2004 Dec 28;43(51):16311-9. [Article]
  7. Ellis MJ, Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS: Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase. Inorg Chem. 2004 Nov 29;43(24):7591-3. [Article]
  8. Hough MA, Ellis MJ, Antonyuk S, Strange RW, Sawers G, Eady RR, Samar Hasnain S: High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. J Mol Biol. 2005 Jul 8;350(2):300-9. [Article]
  9. Paraskevopoulos K, Hough MA, Sawers RG, Eady RR, Hasnain SS: The structure of the Met144Leu mutant of copper nitrite reductase from Alcaligenes xylosoxidans provides the first glimpse of a protein-protein complex with azurin II. J Biol Inorg Chem. 2007 Aug;12(6):789-96. Epub 2007 May 15. [Article]
  10. Hough MA, Eady RR, Hasnain SS: Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants. Biochemistry. 2008 Dec 23;47(51):13547-53. doi: 10.1021/bi801369y. [Article]
  11. Sato K, Firbank SJ, Li C, Banfield MJ, Dennison C: The importance of the long type 1 copper-binding loop of nitrite reductase for structure and function. Chemistry. 2008;14(19):5820-8. doi: 10.1002/chem.200701997. [Article]
  12. Hough MA, Antonyuk SV, Strange RW, Eady RR, Hasnain SS: Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase. J Mol Biol. 2008 Apr 25;378(2):353-61. doi: 10.1016/j.jmb.2008.01.097. Epub 2008 Feb 12. [Article]
  13. Ellis MJ, Buffey SG, Hough MA, Hasnain SS: On-line optical and X-ray spectroscopies with crystallography: an integrated approach for determining metalloprotein structures in functionally well defined states. J Synchrotron Radiat. 2008 Sep;15(Pt 5):433-9. doi: 10.1107/S0909049508014945. Epub 2008 Jul 22. [Article]
  14. Nojiri M, Koteishi H, Nakagami T, Kobayashi K, Inoue T, Yamaguchi K, Suzuki S: Structural basis of inter-protein electron transfer for nitrite reduction in denitrification. Nature. 2009 Nov 5;462(7269):117-20. doi: 10.1038/nature08507. [Article]
  15. Leferink NG, Han C, Antonyuk SV, Heyes DJ, Rigby SE, Hough MA, Eady RR, Scrutton NS, Hasnain SS: Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase. Biochemistry. 2011 May 17;50(19):4121-31. doi: 10.1021/bi200246f. Epub 2011 Apr 19. [Article]
  16. Leferink NG, Antonyuk SV, Houwman JA, Scrutton NS, Eady RR, Hasnain SS: Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase. Nat Commun. 2014 Jul 15;5:4395. doi: 10.1038/ncomms5395. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03088Pidolic acidapproved, investigationalunknownDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails