3.D.4.4.1 Cytochrome oxidase including heme A synthase (HAS) and 4 subunits of the cytochrome oxidase. The 3-d structure of heme A synthase (of 306 aas and 8 TMSs) at 2.2 Å resolution has been solved revealing that the N- and C-terminal halves of HAS consist of four-helix bundles and they align in a pseudo twofold symmetry manner. Each bundle contains a pair of histidine residues and forms a heme-binding domain. The C-half domain binds a cofactor-heme molecule, while the N-half domain is vacant (Niwa et al. 2018). The Sco1 protein, YpmQ, is an accessory protein involved in the assembly of cytochrome c oxidase (Andrews et al. 2004).
|
Accession Number: | P24013 |
Protein Name: | Cytochrome c oxidase subunit 4B |
Length: | 110 |
Molecular Weight: | 12620.00 |
Species: | Bacillus subtilis [1423] |
Number of TMSs: | 3 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
hydron |
---|
Entrez Gene ID: |
936259
|
Pfam: |
PF03626
|
KEGG: |
bsu:BSU14920
|
|
[1] “The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved protein theme.” Saraste M. et.al. 1847686
[2] “The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.” Kunst F. et.al. 9384377
|
1: MVDKKSRGHI NSDLEFKKKK HAREMKYQVL SFGLMIGLTI VAFLTVATDG VGSWFTIPFI
61: ILLAAIQVIF QLYYFMHMNQ KGHEAPALFL YSGVFVAFIT VLAFVTIIWW