Ubiquinol oxidase subunit 1 (P0ABI8)

Identification
Name:Ubiquinol oxidase subunit 1
Synonyms:
  • Cytochrome o subunit 1
  • Cytochrome o ubiquinol oxidase subunit 1
  • Oxidase BO(3) subunit 1
  • Ubiquinol oxidase chain A
  • Ubiquinol oxidase polypeptide I
Gene Name:cyoB
Enzyme Class:Not Available
Biological Properties
General Function:Involved in cytochrome-c 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. This ubiquinol oxidase shows proton pump activity across the membrane in addition to the electron transfer
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 part
Function
binding
catalytic activity
cation binding
electron carrier activity
heme binding
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
aerobic respiration
cellular metabolic process
cellular respiration
energy derivation by oxidation of organic compounds
generation of precursor metabolites and energy
metabolic process
oxidation reduction
Gene Properties
Blattner:b0431
Gene OrientationCounterclockwise
Centisome Percentage:9.65
Left Sequence End447874
Right Sequence End449865
Gene Sequence:
>1992 bp
ATGTTCGGAAAATTATCACTTGATGCAGTCCCGTTCCATGAACCTATCGTCATGGTTACG
ATCGCTGGCATTATTTTGGGAGGTCTGGCGCTCGTTGGCCTGATCACTTACTTCGGTAAG
TGGACCTACCTGTGGAAAGAGTGGCTGACCTCCGTCGACCATAAACGCCTCGGTATCATG
TATATCATCGTGGCGATTGTGATGTTGCTGCGTGGTTTTGCTGACGCCATTATGATGCGT
AGCCAGCAGGCTCTTGCCTCGGCGGGCGAAGCGGGCTTCCTGCCACCTCACCACTACGAT
CAGATCTTTACCGCGCACGGCGTGATTATGATCTTCTTCGTGGCGATGCCTTTCGTTATC
GGTCTGATGAACCTGGTGGTTCCGCTGCAGATCGGCGCGCGTGACGTTGCGTTCCCGTTC
CTCAACAACTTAAGCTTCTGGTTTACCGTTGTTGGTGTGATTCTGGTTAACGTTTCTCTC
GGCGTGGGCGAATTTGCGCAGACCGGCTGGCTGGCCTATCCACCGCTATCGGGAATAGAG
TACAGTCCGGGAGTCGGTGTCGATTACTGGATATGGAGTCTCCAGCTATCCGGTATAGGT
ACGACGCTTACCGGTATCAACTTCTTCGTTACCATTCTGAAGATGCGCGCACCGGGCATG
ACCATGTTCAAGATGCCAGTATTTACCTGGGCATCACTGTGCGCGAACGTACTGATTATT
GCTTCCTTCCCAATTCTGACGGTTACCGTCGCGTTGTTGACCCTGGATCGCTATCTGGGC
ACCCATTTCTTTACCAACGATATGGGTGGCAACATGATGATGTACATCAACCTGATTTGG
GCCTGGGGCCACCCGGAAGTTTACATCCTGATCCTGCCTGTTTTCGGTGTGTTCTCCGAA
ATTGCGGCAACCTTCTCGCGTAAACGTCTGTTTGGTTATACCTCGCTGGTATGGGCAACC
GTCTGTATCACCGTGCTGTCGTTCATCGTTTGGCTGCACCACTTCTTTACGATGGGTGCG
GGCGCGAACGTAAACGCCTTCTTTGGTATCACCACAATGATTATCGCCATCCCGACCGGG
GTGAAGATCTTCAACTGGCTGTTCACCATGTATCAGGGCCGCATCGTGTTCCATTCTGCG
ATGCTGTGGACCATCGGTTTTATCGTCACCTTCTCGGTGGGCGGGATGACTGGCGTGCTG
CTGGCCGTACCGGGCGCGGACTTCGTTCTGCATAACAGCCTGTTCCTGATTGCGCACTTC
CATAACGTGATCATCGGCGGCGTGGTCTTCGGCTGCTTCGCAGGGATGACCTACTGGTGG
CCTAAAGCGTTCGGTTTCAAACTGAACGAAACCTGGGGTAAACGCGCGTTCTGGTTCTGG
ATCATCGGCTTCTTCGTTGCCTTTATGCCACTGTATGCGCTGGGCTTCATGGGCATGACC
CGTCGTTTGAGCCAGCAGATTGACCCGCAGTTCCACACCATGCTGATGATTGCAGCCAGC
GGTGCAGTACTGATTGCGCTGGGTATTCTCTGCCTCGTTATTCAGATGTACGTTTCTATT
CGCGACCGCGACCAGAACCGTGACCTGACTGGCGACCCGTGGGGTGGCCGTACGCTGGAG
TGGGCAACCTCTTCCCCGCCTCCGTTCTATAACTTTGCCGTAGTGCCGCACGTTCACGAA
CGTGATGCATTCTGGGAAATGAAAGAGAAAGGCGAAGCGTATAAAAAGCCTGACCACTAT
GAAGAAATTCATATGCCGAAAAACAGCGGTGCAGGTATCGTCATTGCAGCTTTCTCCACC
ATCTTCGGTTTCGCCATGATCTGGCATATCTGGTGGCTGGCGATTGTTGGCTTCGCAGGC
ATGATCATCACCTGGATCGTGAAAAGCTTCGACGAGGACGTGGATTACTACGTGCCGGTG
GCAGAAATCGAAAAACTGGAAAACCAGCATTTCGATGAGATTACTAAGGCAGGGCTGAAA
AATGGCAACTGA
Protein Properties
Pfam Domain Function:
Protein Residues:663
Protein Molecular Weight:74367
Protein Theoretical pI:7
PDB File:1FFT
Signaling Regions:
  • None
Transmembrane Regions:
  • 17-35
  • 53-80
  • 96-132
  • 138-161
  • 185-215
  • 225-260
  • 271-307
  • 312-326
  • 341-369
  • 378-409
  • 413-445
  • 449-477
  • 490-521
  • 588-606
  • 614-632
Protein Sequence:
>Ubiquinol oxidase subunit 1
MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIM
YIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVI
GLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIE
YSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII
ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSE
IAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG
VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHF
HNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT
RRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLE
WATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFST
IFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLK
NGN
References
External Links:
ResourceLink
Uniprot ID:P0ABI8
Uniprot Name:CYOB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674571
PDB ID:1FFT
Ecogene ID:EG10179
Ecocyc:EG10179
ColiBase:b0431
Kegg Gene:b0431
EchoBASE ID:EB0176
CCDB:CYOB_ECOLI
BacMap:16128416
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
  • Kawasaki, M., Mogi, T., Anraku, Y. (1997). "Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase." J Biochem 122:422-429. Pubmed: 9378723