Cytochrome c-552

Details

Name
Cytochrome c-552
Synonyms
  • 1.7.2.2
  • Cytochrome c nitrite reductase
  • TvNiR
Gene Name
nir
Organism
Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)
Amino acid sequence
>lcl|BSEQ0019555|Cytochrome c-552
MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHAT
VNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKAT
PTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAV
RGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTS
EVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKV
TFQRGREDFRAIGLLDTADSNVMCAQCHVEYNCNPGYQLSDGSRVGMDDRRANHFFWANV
FDYKEAAQEIDFFDFRHATTGAALPKLQHPEAETFWGSVHERNGVACADCHMPKVQLENG
KVYTSHSQRTPRDMMGQACLNCHAEWTEDQALYAIDYIKNYTHGKIVKSEYWLAKMIDLF
PVAKRAGVSEDVLNQARELHYDAHLYWEWWTAENSVGFHNPDQARESLMTSISKSKEAVS
LLNDAIDAQVASR
Number of residues
553
Molecular Weight
62344.36
Theoretical pI
6.35
GO Classification
Functions
calcium ion binding / heme binding / nitrite reductase (cytochrome, ammonia-forming) activity
Processes
ammonium ion metabolic process / nitrate assimilation
Components
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:16500161, PubMed:22281743). Has very low activity toward hydroxylamine (PubMed:16500161). Has even lower activity toward sulfite (PubMed:16500161, PubMed:22281743). Sulfite reductase activity is maximal at neutral pH (PubMed:20944237).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0019556|Cytochrome c-552 (nir)
ATGAATGATCTCAACAGACTCGGCCGTGTGGGCCGATGGATTGCGGGGGCAGCCTGTCTG
TTCCTTGCCTCTGCCGCTCACGCGGAACCGGGGGAGAACCTCAAACCCGTGGATGCGATG
CAGTGCTTCGACTGCCACACGCAGATCGAGGACATGCACACAGTTGGCAAGCACGCCACC
GTGAACTGTGTCCACTGTCACGATGCTACCGAGCACGTCGAAACGGCCAGCAGCCGCCGC
ATGGGCGAACGGCCCGTTACACGCATGGATCTGGAGGCCTGCGCTACCTGCCATACCGCA
CAGTTCAATTCCTTCGTTGAAGTGCGCCACGAGTCGCACCCGCGCTTGGAGAAGGCGACG
CCGACGAGTCGGTCGCCGATGTTCGACAAGCTGATCGCCGGTCACGGTTTCGCGTTCGAG
CACGCCGAACCGCGCAGTCACGCGTTCATGCTGGTCGATCACTTTGTCGTCGACCGCGCT
TATGGCGGCCGCTTCCAGTTCAAGAACTGGCAGAAGGTCACCGACGGCATGGGGGCGGTT
CGCGGCGCCTGGACAGTGCTGACCGATGCCGACCCCGAGAGCTCGGACCAGCGCCGGTTC
CTGTCGCAGACGGCCACCGCCGCAAACCCGGTGTGCCTGAACTGCAAGACGCAGGACCAT
ATCCTTGACTGGGCCTACATGGGTGACGAGCACGAAGCGGCCAAGTGGAGCCGGACCTCG
GAGGTGGTCGAGTTCGCGCGTGACTTGAACCATCCGCTGAACTGCTTCATGTGCCATGAC
CCGCATTCGGCCGGTCCGCGCGTCGTGCGTGACGGCCTGATCAATGCGGTTGTCGACCGC
GGGCTCGGGACCTACCCGCATGACCCGGTGAAAAGCGAACAGCAGGGCATGACCAAGGTC
ACGTTCCAGCGCGGCCGCGAGGACTTCCGGGCGATCGGCCTGCTCGATACGGCGGATTCC
AACGTGATGTGCGCCCAGTGCCACGTGGAGTACAACTGCAACCCGGGTTACCAGTTGAGT
GACGGGTCGCGGGTCGGCATGGACGATCGTCGCGCCAACCACTTCTTCTGGGCCAACGTG
TTCGACTACAAGGAAGCCGCGCAGGAGATCGACTTCTTCGATTTCCGGCATGCCACCACC
GGAGCGGCGCTGCCGAAGCTGCAGCATCCGGAGGCCGAGACGTTCTGGGGCTCTGTCCAC
GAGCGCAACGGCGTCGCCTGCGCCGACTGCCACATGCCCAAGGTTCAGCTGGAAAACGGC
AAGGTCTACACCAGCCACAGCCAGCGCACGCCGCGTGACATGATGGGCCAGGCGTGTCTG
AACTGCCATGCGGAGTGGACCGAGGATCAGGCCCTGTACGCGATCGACTACATCAAGAAC
TACACTCACGGCAAGATCGTCAAATCCGAGTACTGGCTTGCCAAGATGATCGACCTGTTC
CCGGTCGCGAAGCGGGCTGGCGTGTCGGAGGATGTTCTGAACCAGGCGCGTGAGCTGCAC
TACGACGCACACCTGTACTGGGAGTGGTGGACCGCGGAAAACTCCGTCGGTTTCCACAAC
CCCGATCAGGCGCGTGAGTCGCTGATGACCTCGATCAGCAAGAGCAAGGAAGCCGTTAGC
CTGCTGAATGACGCAATCGACGCCCAGGTGGCTTCGAGATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDL0DSL2
UniProtKB Entry NameNIR_THIND
GenBank Protein ID73661133
GenBank Gene IDAJ880678
General References
  1. Tikhonova TV, Slutsky A, Antipov AN, Boyko KM, Polyakov KM, Sorokin DY, Zvyagilskaya RA, Popov VO: Molecular and catalytic properties of a novel cytochrome c nitrite reductase from nitrate-reducing haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio nitratireducens. Biochim Biophys Acta. 2006 Apr;1764(4):715-23. Epub 2006 Feb 9. [Article]
  2. Polyakov KM, Boyko KM, Tikhonova TV, Slutsky A, Antipov AN, Zvyagilskaya RA, Popov AN, Bourenkov GP, Lamzin VS, Popov VO: High-resolution structural analysis of a novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens. J Mol Biol. 2009 Jun 26;389(5):846-62. doi: 10.1016/j.jmb.2009.04.037. Epub 2009 Apr 23. [Article]
  3. Trofimov AA, Polyakov KM, Boyko KM, Tikhonova TV, Safonova TN, Tikhonov AV, Popov AN, Popov VO: Structures of complexes of octahaem cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens with sulfite and cyanide. Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1043-7. doi: 10.1107/S0907444910031665. Epub 2010 Sep 18. [Article]
  4. Trofimov AA, Polyakov KM, Tikhonova TV, Tikhonov AV, Safonova TN, Boyko KM, Dorovatovskii PV, Popov VO: Covalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activity. Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):144-53. doi: 10.1107/S0907444911052632. Epub 2012 Jan 13. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02580PentaglymeexperimentalunknownDetails