Identification
Name:Cytochrome o ubiquinol oxidase protein cyoD
Synonyms:
  • Ubiquinol oxidase chain D
Gene Name:cyoD
Enzyme Class:Not Available
Biological Properties
General Function:Involved in cytochrome o ubiquinol oxidase activity
Specific Function:Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
SMPDB Reactions:
1.0Thumb+8.0Thumb+2.0Thumb2.0Thumb+8.0Thumb+2.0Thumb
Complex Reactions:
2.0Thumb+0.5Thumb+1.0Thumb1.0Thumb+1.0Thumb+2.0Thumb
4.0Thumb+0.5Thumb+1.0Thumb1.0Thumb+1.0Thumb+4.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB21574Ubiquinol-1MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
Function
catalytic activity
cytochrome o ubiquinol oxidase activity
heme-copper terminal oxidase activity
oxidoreductase activity
Process
electron transport coupled proton transport
energy coupled proton transport, against electrochemical gradient
establishment of localization
hydrogen transport
proton transport
transport
Gene Properties
Blattner:b0429
Gene OrientationCounterclockwise
Centisome Percentage:9.63
Left Sequence End446941
Right Sequence End447270
Gene Sequence:
>330 bp
ATGAGTCATTCTACCGATCACAGCGGCGCGTCCCATGGCAGCGTAAAAACCTACATGACA
GGCTTTATCCTGTCGATCATTCTGACGGTGATTCCGTTCTGGATGGTGATGACAGGAGCT
GCCTCTCCGGCCGTAATTCTGGGAACAATCCTGGCAATGGCAGTGGTACAGGTTCTGGTG
CATCTGGTGTGCTTCCTGCACATGAATACCAAATCAGATGAAGGCTGGAACATGACGGCG
TTTGTCTTCACCGTGCTAATCATCGCTATCCTGGTTGTAGGCTCCATCTGGATTATGTGG
AACCTCAACTACAACATGATGATGCACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:109
Protein Molecular Weight:12029
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • 18-36
  • 46-64
  • 81-99
Protein Sequence:
>Cytochrome o ubiquinol oxidase protein cyoD
MSHSTDHSGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQVLV
HLVCFLHMNTKSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH
References
External Links:
ResourceLink
Uniprot ID:P0ABJ6
Uniprot Name:CYOD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674569
Ecogene ID:EG10181
Ecocyc:EG10181
ColiBase:b0429
Kegg Gene:b0429
EchoBASE ID:EB0178
CCDB:CYOD_ECOLI
BacMap:16128414
General Reference:
  • Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S., Wikstrom, M. (2000). "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol 7:910-917. Pubmed: 11017202
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Chepuri, V., Gennis, R. B. (1990). "The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli." J Biol Chem 265:12978-12986. Pubmed: 2165491
  • Chepuri, V., Lemieux, L., Au, D. C., Gennis, R. B. (1990). "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem 265:11185-11192. Pubmed: 2162835
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553