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
- Functionscalcium ion binding / heme binding / nitrite reductase (cytochrome, ammonia-forming) activityProcessesammonium ion metabolic process / nitrate assimilationComponentsperiplasmic 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
- Cytochrom_C552 (PF02335)
- 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
Resource Link UniProtKB ID L0DSL2 UniProtKB Entry Name NIR_THIND GenBank Protein ID 73661133 GenBank Gene ID AJ880678 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 ID tni:TVNIR_0259 - General References
- 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]
- 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]
- 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]
- 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
Drug Drug group Pharmacological action? Type Actions Details Pentaglyme experimental unknown target Details