Cytochrome c-552
Details
- Name
- Cytochrome c-552
- Synonyms
- 1.-.-.-
- Gene Name
- Not Available
- Organism
- Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
- Amino acid sequence
>lcl|BSEQ0012875|Cytochrome c-552 MNNQKTFKGLRLAALGLVAVAAFTAGCSDVSTELKTPVYKTKLTAEEIRNSAFKPEFPKQ YASYERNDETTVMTEYKGSVPFNKNDNVNPLPEGYRHAQPYLKNLWLGYPFMYEYREARG HTYAIQDFLHIDRINRYAEKGGLPATCWNCKTPKMMEWVKESGDGFWAKDVNEFRDKIDM KDHTIGCATCHDPQTMELRITSVPLTDYLVSQGKDPKKLPRNEMRALVCGQCHVEYYFNG PTMGVNKKPVFPWAEGFDPADMYRYYDKHGDLQVKGFEGKFADWTHPASKTPMIKAQHPE YETWINGTHGAAGVTCADCHMSYTRSDDKKKISSHWWTSPMKDPEMRACRQCHSDKTPDY LKSRVLFTQKRTFDLLLAAQEVSVKAHEAVRLANEYQGAKAAGYDDLMIQAREMVRKGQF FWDYVSAENSVGFHNPAKALDTLAQSQQFSQKAIDLAMEATQYGIGKDLSGDIKTIVPPI LKMNRKLQQDPEFMKTHKWFQYLPVLPKADQVWDGQKRLVSAKQ
- Number of residues
- 524
- Molecular Weight
- 60002.975
- Theoretical pI
- 8.54
- GO Classification
- Functionsmetal ion binding / nitrite reductase (cytochrome, ammonia-forming) activityProcessesnitrate assimilationComponentsperiplasmic space
- General Function
- Nitrite reductase (cytochrome, ammonia-forming) activity
- Specific Function
- Not Available
- Pfam Domain Function
- Cytochrom_C552 (PF02335)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0012876|Cytochrome c-552 ATGAATAACCAGAAGACGTTCAAGGGGTTGCGCCTCGCCGCGCTGGGACTCGTGGCCGTG GCCGCCTTCACCGCAGGGTGTTCCGACGTGTCCACCGAACTCAAGACCCCCGTGTACAAG ACGAAACTGACGGCGGAGGAAATCCGCAACAGCGCCTTCAAGCCCGAGTTTCCCAAGCAG TACGCCAGCTACGAGCGTAACGACGAGACTACGGTGATGACCGAATACAAGGGGTCTGTG CCGTTCAACAAGAACGACAACGTGAATCCCCTGCCTGAAGGCTACAGGCACGCGCAGCCG TACCTGAAGAACCTCTGGCTCGGCTATCCCTTCATGTACGAGTACCGTGAGGCGCGGGGC CATACCTACGCCATTCAGGACTTCCTGCACATCGACCGTATCAATCGCTACGCGGAGAAA GGCGGACTGCCCGCCACCTGCTGGAACTGCAAGACCCCCAAGATGATGGAGTGGGTCAAG GAGAGCGGCGACGGCTTCTGGGCGAAGGACGTCAACGAATTCCGCGACAAGATCGACATG AAGGATCACACCATCGGGTGTGCCACCTGTCACGACCCCCAGACCATGGAACTGCGCATC ACCAGCGTGCCGCTCACCGACTACCTCGTCTCGCAGGGCAAGGACCCCAAGAAGCTGCCG CGTAACGAGATGCGCGCACTGGTATGCGGTCAGTGCCACGTGGAGTACTACTTCAACGGC CCCACCATGGGCGTGAACAAGAAGCCGGTGTTCCCGTGGGCCGAGGGTTTCGACCCTGCC GACATGTATCGCTACTACGACAAGCACGGCGACCTGCAGGTGAAGGGCTTCGAGGGCAAG TTCGCGGACTGGACGCACCCGGCTTCCAAGACCCCCATGATCAAGGCCCAGCACCCCGAA TACGAGACGTGGATCAACGGCACCCACGGGGCCGCTGGCGTCACCTGCGCCGACTGCCAC ATGAGCTACACCCGCAGCGACGACAAGAAGAAGATATCGTCGCACTGGTGGACTTCGCCC ATGAAGGACCCCGAAATGCGTGCCTGCCGCCAGTGCCACTCCGATAAGACCCCCGACTAC CTCAAGTCGCGCGTGCTCTTCACCCAGAAGCGCACCTTCGACCTGTTGCTGGCGGCGCAG GAGGTGTCGGTGAAGGCGCATGAAGCGGTACGCCTTGCCAACGAATACCAGGGCGCCAAG GCCGCAGGCTATGACGACCTGATGATCCAGGCCCGTGAGATGGTCCGCAAGGGACAGTTC TTCTGGGACTACGTGTCCGCCGAAAACAGCGTGGGCTTCCACAACCCCGCCAAGGCACTC GACACGCTGGCCCAGTCGCAGCAGTTCAGCCAGAAGGCCATCGACCTCGCCATGGAAGCG ACCCAGTACGGCATCGGCAAGGACCTTTCGGGCGACATCAAGACCATCGTGCCGCCCATC CTGAAGATGAACCGCAAGCTGCAGCAGGACCCGGAATTCATGAAGACCCACAAGTGGTTC CAGTACCTGCCCGTGCTGCCCAAGGCCGATCAGGTGTGGGACGGACAGAAGCGTCTGGTC TCCGCCAAGCAGTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q72EF3 UniProtKB Entry Name Q72EF3_DESVH GenBank Protein ID 46447829 GenBank Gene ID AE017285 - General References
- Rodrigues ML, Oliveira TF, Pereira IA, Archer M: X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination. EMBO J. 2006 Dec 13;25(24):5951-60. Epub 2006 Nov 30. [Article]
- Rodrigues ML, Scott KA, Sansom MS, Pereira IA, Archer M: Quinol oxidation by c-type cytochromes: structural characterization of the menaquinol binding site of NrfHA. J Mol Biol. 2008 Aug 29;381(2):341-50. doi: 10.1016/j.jmb.2008.05.066. Epub 2008 Jun 3. [Article]