Ubiquinol oxidase subunit 2 (P0ABJ1)

Identification
Name:Ubiquinol oxidase subunit 2
Synonyms:
  • Cytochrome o subunit 2
  • Cytochrome o ubiquinol oxidase subunit 2
  • Ubiquinol oxidase chain B
  • Oxidase BO(3) subunit 2
  • Ubiquinol oxidase polypeptide II
Gene Name:cyoA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in cytochrome bo3 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+2.0Thumb → 2.0Thumb+8.0Thumb+2.0Thumb
1.0Oxygen + 8.0Hydrogen ion + 2.0Ubiquinol-1 → 2.0Water + 8.0Hydrogen ion + 2.0Ubiquinone-1
ReactionCard
Complex Reactions:
2.0Thumb+0.5Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+2.0Thumb
2.0Hydrogen ion + 0.5Oxygen + 1.0Ubiquinol-8 → 1.0Water + 1.0Ubiquinone-8 + 2.0Hydrogen ion
ReactionCard
4.0Thumb+0.5Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+4.0Thumb
4.0Hydrogen ion + 0.5Oxygen + 1.0Ubiquinol-8 → 1.0Water + 1.0Ubiquinone-8 + 4.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB21574Ubiquinol-1MetaboCard
ECMDB21579Ubiquinol-7MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21580Ubiquinol-9MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane
membrane part
Function
binding
catalytic activity
cation binding
copper ion binding
cytochrome bo3 ubiquinol oxidase activity
cytochrome o ubiquinol oxidase activity
cytochrome-c oxidase activity
electron carrier activity
heme binding
heme-copper terminal oxidase activity
ion binding
iron ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on diphenols and related substances as donors
oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
transition metal ion binding
Process
cellular metabolic process
electron transport chain
generation of precursor metabolites and energy
metabolic process
oxidation reduction
respiratory electron transport chain
Gene Properties
Blattner:b0432
Gene OrientationCounterclockwise
Centisome Percentage:9.70
Left Sequence End449887
Right Sequence End450834
Gene Sequence:
>948 bp
ATGAGACTCAGGAAATACAATAAAAGTTTGGGATGGTTGTCATTATTTGCAGGCACTGTA
TTGCTCAGTGGCTGTAATTCTGCGCTGTTAGATCCCAAAGGACAGATTGGTCTGGAGCAA
CGTTCACTGATACTGACGGCATTTGGCCTGATGTTGATTGTCGTTATTCCCGCAATCTTG
ATGGCTGTTGGTTTCGCCTGGAAGTACCGTGCGAGCAATAAAGATGCTAAGTACAGCCCG
AACTGGTCACACTCCAATAAAGTGGAAGCTGTGGTCTGGACGGTACCTATCTTAATCATC
ATCTTCCTTGCAGTACTGACCTGGAAAACCACTCACGCTCTTGAGCCTAGCAAGCCGCTG
GCACACGACGAGAAGCCCATTACCATCGAAGTGGTTTCCATGGACTGGAAATGGTTCTTC
ATCTACCCGGAACAGGGCATTGCTACCGTGAATGAAATCGCTTTCCCGGCGAACACTCCG
GTGTACTTCAAAGTGACCTCCAACTCCGTGATGAACTCCTTCTTCATTCCGCGTCTGGGT
AGCCAGATTTATGCCATGGCCGGTATGCAGACTCGCCTGCATCTGATCGCCAACGAACCC
GGCACTTATGACGGTATCTCCGCCAGCTACAGCGGCCCGGGCTTCTCAGGCATGAAGTTC
AAAGCTATTGCAACACCGGATCGCGCCGCATTCGACCAGTGGGTCGCAAAAGCGAAGCAG
TCGCCGAACACCATGTCTGACATGGCTGCGTTCGAAAAACTGGCCGCGCCTAGCGAATAC
AACCAGGTGGAATATTTCTCCAACGTGAAACCAGACTTGTTTGCCGATGTAATTAACAAG
TTTATGGCTCACGGTAAGAGCATGGACATGACCCAGCCAGAAGGTGAGCACAGCGCACAC
GAAGGTATGGAAGGCATGGACATGAGCCACGCGGAATCCGCCCATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:315
Protein Molecular Weight:34911
Protein Theoretical pI:7
PDB File:1FFT
Signaling Regions:
  • 1-24
Transmembrane Regions:
  • 51-68
  • 93-111
Protein Sequence:
>Ubiquinol oxidase subunit 2
MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAIL
MAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPL
AHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLG
SQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQ
SPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAH
EGMEGMDMSHAESAH
References
External Links:
ResourceLink
Uniprot ID:P0ABJ1
Uniprot Name:CYOA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674572
PDB ID:1FFT
Ecogene ID:EG10178
Ecocyc:EG10178
ColiBase:b0432
Kegg Gene:b0432
EchoBASE ID:EB0175
CCDB:CYOA_ECOLI
BacMap:16128417
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
  • Chepuri, V., Lemieux, L., Hill, J., Alben, J. O., Gennis, R. B. (1990). "Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli." Biochim Biophys Acta 1018:124-127. Pubmed: 2168206
  • 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
  • Lindquist, S., Weston-Hafer, K., Schmidt, H., Pul, C., Korfmann, G., Erickson, J., Sanders, C., Martin, H. H., Normark, S. (1993). "AmpG, a signal transducer in chromosomal beta-lactamase induction." Mol Microbiol 9:703-715. Pubmed: 8231804
  • Minagawa, J., Nakamura, H., Yamato, I., Mogi, T., Anraku, Y. (1990). "Transcriptional regulation of the cytochrome b562-o complex in Escherichia coli. Gene expression and molecular characterization of the promoter." J Biol Chem 265:11198-11203. Pubmed: 2162837
  • Minghetti, K. C., Goswitz, V. C., Gabriel, N. E., Hill, J. J., Barassi, C. A., Georgiou, C. D., Chan, S. I., Gennis, R. B. (1992). "Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity." Biochemistry 31:6917-6924. Pubmed: 1322173
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137
  • Wilmanns, M., Lappalainen, P., Kelly, M., Sauer-Eriksson, E., Saraste, M. (1995). "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center." Proc Natl Acad Sci U S A 92:11955-11959. Pubmed: 8618822