Cytochrome c oxidase subunit 2

Details

Name
Cytochrome c oxidase subunit 2
Synonyms
  • 1.9.3.1
  • coiI
  • ctaB
  • Cytochrome aa3 subunit 2
  • Cytochrome c oxidase polypeptide II
  • Oxidase aa(3) subunit 2
Gene Name
ctaC
Organism
Paracoccus denitrificans
Amino acid sequence
>lcl|BSEQ0012898|Cytochrome c oxidase subunit 2
MMAIATKRRGVAAVMSLGVATMTAVPALAQDVLGDLPVIGKPVNGGMNFQPASSPLAHDQ
QWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANPVPARFTHNTPIEVIWTLVPVLILVA
IGAFSLPILFRSQEMPNDPDLVIKAIGHQWYWSYEYPNDGVAFDALMLEKEALADAGYSE
DEYLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGV
YFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEEFAADASDYLPASPVKLASAE
Number of residues
298
Molecular Weight
32538.495
Theoretical pI
4.7
GO Classification
Functions
copper ion binding / cytochrome-c oxidase activity
Processes
electron transport chain
Components
integral component of membrane / plasma membrane / respiratory chain
General Function
Cytochrome-c oxidase activity
Specific Function
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Pfam Domain Function
Transmembrane Regions
56-88 104-134
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0007921|897 bp
ATGATGGCAATTGCGACCAAGCGCCGCGGGGTGGCGGCGGTGATGAGCCTGGGAGTTGCG
ACGATGACGGCCGTGCCGGCCTTGGCGCAGGACGTGCTGGGCGATCTGCCGGTGATCGGC
AAGCCGGTGAACGGCGGGATGAACTTCCAACCGGCGTCGAGCCCGCTGGCGCATGACCAG
CAATGGCTGGATCATTTCGTGCTCTACATCATCACGGCCGTGACGATCTTCGTCTGCCTG
CTGCTGCTGATCTGCATCGTCCGTTTCAACCGCCGGGCGAATCCGGTGCCGGCGCGCTTT
ACCCACAACACCCCGATCGAGGTGATCTGGACCCTGGTCCCGGTGCTGATCCTGGTGGCG
ATCGGGGCCTTCTCGCTGCCGATCCTGTTCCGCAGCCAGGAGATGCCGAACGATCCCGAC
CTGGTGATCAAGGCCATCGGCCACCAGTGGTACTGGTCCTATGAATACCCCAATGACGGC
GTCGCCTTCGACGCGCTGATGCTGGAGAAAGAGGCCCTGGCCGATGCCGGCTATTCCGAG
GACGAGTATCTGCTGGCGACCGACAACCCGGTCGTGGTTCCGGTCGGCAAGAAGGTCCTG
GTCCAGGTGACCGCGACCGACGTGATCCACGCCTGGACCATCCCCGCCTTCGCCGTCAAG
CAGGACGCCGTGCCGGGCCGCATCGCGCAGCTGTGGTTCTCGGTCGACCAGGAGGGCGTC
TATTTCGGCCAGTGCTCCGAGCTTTGCGGCATCAACCACGCCTATATGCCCATCGTCGTC
AAGGCGGTCAGCCAGGAGAAATACGAAGCCTGGCTTGCCGGCGCGAAAGAGGAATTCGCC
GCCGACGCCTCGGACTACCTGCCCGCCAGCCCCGTCAAGCTGGCCTCGGCAGAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP08306
UniProtKB Entry NameCOX2_PARDE
GenBank Protein ID45469
GenBank Gene IDX05828
General References
  1. Raitio M, Jalli T, Saraste M: Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans. EMBO J. 1987 Sep;6(9):2825-33. [Article]
  2. Steinrucke P, Steffens GC, Panskus G, Buse G, Ludwig B: Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein. Eur J Biochem. 1987 Sep 15;167(3):431-9. [Article]
  3. Iwata S, Ostermeier C, Ludwig B, Michel H: Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 1995 Aug 24;376(6542):660-9. [Article]
  4. Ostermeier C, Harrenga A, Ermler U, Michel H: Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc Natl Acad Sci U S A. 1997 Sep 30;94(20):10547-53. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04147Dodecyldimethylamine N-oxideexperimentalunknownDetails