Cytochrome c oxidase subunit 1-beta

Details

Name
Cytochrome c oxidase subunit 1-beta
Synonyms
  • 1.9.3.1
  • Cytochrome aa3 subunit 1-beta
  • Cytochrome c oxidase polypeptide I-beta
Gene Name
ctaDII
Organism
Paracoccus denitrificans
Amino acid sequence
>lcl|BSEQ0017350|Cytochrome c oxidase subunit 1-beta
MADAAVHGHGDHHDTRGFFTRWFMSTNHKDIGILYLFTAGIVGLISVCFTVYMRMELQHP
GVQYMCLEGARLIADASAECTPNGHLWNVMITYHGVLMMFFVVIPALFGGFGNYFMPLHI
GAPDMAFPRLNNLSYWMYVCGVALGVASLLAPGGNDQMGSGVGWVLYPPLSTTEAGYSMD
LAIFAVHVSGASSILGAINIITTFLNMRAPGMTLFKVPLFAWSVFITAWLILLSLPVLAG
AITMLLMDRNFGTQFFDPAGGGDPVLYQHILWFFGHPEVYIIILPGFGIISHVISTFAKK
PIFGYLPMVLAMAAIGILGFVVWAHHMYTAGMSLTQQAYFMLATMTIAVPTGIKVFSWIA
TMWGGSIEFKTPMLWAFGFLFLFTVGGVTGVVLSQAPLDRVYHDTYYVVAHFHYVMSLGA
VFGIFAGVYYWIGKMSGRQYPEWAGQLHFWMMFIGSNLIFFPQHFLGRQGMPRRYIDYPV
EFAYWNNISSIGAYISFASFLFFIGIVFYTLFAGKRVNVPNYWNEHADTLEWTLPSPPPE
HTFETLPKREDWDRAHAH
Number of residues
558
Molecular Weight
62438.635
Theoretical pI
6.97
GO Classification
Functions
copper ion binding / cytochrome-c oxidase activity / heme binding / iron ion binding
Processes
aerobic respiration / electron transport chain / oxidative phosphorylation
Components
integral component of membrane / plasma membrane / respiratory chain
General Function
Iron ion binding
Specific Function
Subunit 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). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
Pfam Domain Function
Transmembrane Regions
29-59 83-120 127-151 177-206 218-251 263-299 304-331 333-364 370-395 405-437 441-469 479-514
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0007919|468 bp
ATGAAGATCAGCATCTATGCCACTCTCGCCGCCATCACCCTCGCCCTGCCCGCTGCGGCC
CAGGATGGCGACGCCGCCAAAGGCGAGAAAGAATTCAACAAGTGCAAGGCTTGCCACATG
ATCCAGGCGCCGGACGGCACCGACATCATCAAGGGCGGCAAGACCGGGCCCAACCTTTAC
GGCGTCGTCGGCCGCAAGATCGCCTCGGAGGAGGGCTTCAAATACGGCGAAGGCATCCTC
GAGGTCGCCGAAAAGAACCCCGACCTGACCTGGACCGAGGCCGACCTGATCGAATACGTC
ACCGACCCCAAGCCCTGGCTGGTCAAGATGACCGACGACAAGGGCGCCAAGACCAAGATG
ACCTTCAAGATGGGCAAGAACCAGGCCGACGTGGTGGCCTTCCTGGCCCAGAACTCGCCC
GATGCGGGCGGCGACGGCGAGGCTGCGGCCGAGGGCGAATCGAACTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP98002
UniProtKB Entry NameCOX1B_PARDE
GenBank Protein ID45478
GenBank Gene IDY07533
General References
  1. Raitio M, Pispa JM, Metso T, Saraste M: Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans? FEBS Lett. 1990 Feb 26;261(2):431-5. [Article]
  2. 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]
  3. 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]
  4. Buse G, Soulimane T, Dewor M, Meyer HE, Bluggel M: Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase. Protein Sci. 1999 May;8(5):985-90. [Article]
  5. Ostermeier C, Iwata S, Michel H: Cytochrome c oxidase. Curr Opin Struct Biol. 1996 Aug;6(4):460-6. [Article]

Drug Relations

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