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
Functions
metal ion binding / nitrite reductase (cytochrome, ammonia-forming) activity
Processes
nitrate assimilation
Components
periplasmic space
General Function
Nitrite reductase (cytochrome, ammonia-forming) activity
Specific Function
Not Available
Pfam Domain Function
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
ResourceLink
UniProtKB IDQ72EF3
UniProtKB Entry NameQ72EF3_DESVH
GenBank Protein ID46447829
GenBank Gene IDAE017285
General References
  1. 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]
  2. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB079182-heptyl-4-hydroxyquinoline N-oxideexperimentalunknownDetails