Cytochrome c-552

Details

Name
Cytochrome c-552
Kind
protein
Synonyms
  • 1.7.2.2
  • Cytochrome c nitrite reductase
  • TvNiR
Gene Name
nir
UniProtKB Entry
L0DSL2Swiss-Prot
Organism
Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)
NCBI Taxonomy ID
1255043
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
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).
Specific Function
calcium ion binding
Pfam Domain Function
Signal Regions
1-28
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
PDB ID(s)2OT4, 2ZO5, 3D1I, 3F29, 3FO3, 3GM6, 3LG1, 3LGQ, 3MMO, 3OWM, 3RKH, 3S7W, 3SCE, 3UU9, 4L38, 4L3X, 4L3Y, 4L3Z, 4Q0T, 4Q17, 4Q1O, 4Q4U, 4Q5B, 4Q5C
KEGG IDtni:TVNIR_0259
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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
PentaglymeexperimentalunknowntargetDetails