Blue copper oxidase cueO (P36649)

Identification
Name:Blue copper oxidase cueO
Synonyms:
  • Copper efflux oxidase
Gene Name:cueO
Enzyme Class:Not Available
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm
Cellular Location:Periplasm.
SMPDB Pathways:
KEGG Pathways:Not Available
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Pyrocatechuic acid + 1.0Oxygen → 1.0Hydrogen ion + 1.02-Carboxymuconate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Fe3++1.0Thumb
1.0Iron + 1.0Hydrogen ion + 1.0Oxygen → 1.0Fe3+ + 1.0Water
ReactionCard
1.0Cu++1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cu+ + 1.0Hydrogen ion + 1.0Oxygen → 1.0Copper + 1.0Water
ReactionCard
Complex Reactions:
4.0Thumb+4.0Thumb+1.0Thumb → 4.0Thumb+2.0Thumb
4.0Copper + 4.0Hydrogen ion + 1.0Oxygen → 4.0Copper + 2.0Water
ReactionCard
4.0Thumb+4.0Thumb+1.0Thumb → 4.0Thumb+2.0Thumb
4.0Iron + 4.0Hydrogen ion + 1.0Oxygen → 4.0Fe3+ + 2.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB202242-CarboxymuconateMetaboCard
ECMDB003972-Pyrocatechuic acidMetaboCard
ECMDB00657CopperMetaboCard
ECMDB21395Fe3+MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00692IronMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
copper ion binding
ion binding
metal ion binding
oxidoreductase activity
transition metal ion binding
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0123
Gene OrientationClockwise
Centisome Percentage:2.95
Left Sequence End137083
Right Sequence End138633
Gene Sequence:
>1551 bp
ATGCAACGTCGTGATTTCTTAAAATATTCCGTCGCGCTGGGTGTGGCTTCGGCTTTGCCG
CTGTGGAGCCGCGCAGTATTTGCGGCAGAACGCCCAACGTTACCGATCCCTGATTTGCTC
ACGACCGATGCCCGTAATCGCATTCAGTTAACTATTGGCGCAGGCCAGTCCACCTTTGGC
GGGAAAACTGCAACTACCTGGGGCTATAACGGCAATCTGCTGGGGCCGGCGGTGAAATTA
CAGCGCGGCAAAGCGGTAACGGTTGATATCTACAACCAACTGACGGAAGAGACAACGTTG
CACTGGCACGGGCTGGAAGTACCGGGTGAAGTCGACGGCGGCCCGCAGGGAATTATTCCG
CCAGGTGGCAAGCGCTCGGTGACGTTGAACGTTGATCAACCTGCCGCTACCTGCTGGTTC
CATCCGCATCAGCACGGCAAAACCGGGCGACAGGTGGCGATGGGGCTGGCTGGGCTGGTG
GTGATTGAAGATGACGAGATCCTGAAATTAATGCTGCCAAAACAGTGGGGTATCGATGAT
GTTCCGGTGATCGTTCAGGATAAGAAATTTAGCGCCGACGGGCAGATTGATTATCAACTG
GATGTGATGACCGCCGCCGTGGGCTGGTTTGGCGATACGTTGCTGACCAACGGTGCAATC
TACCCGCAACACGCTGCCCCGCGTGGTTGGCTGCGCCTGCGTTTGCTCAATGGCTGTAAT
GCCCGTTCGCTCAATTTCGCCACCAGCGACAATCGCCCGCTGTATGTGATTGCCAGCGAC
GGTGGTCTGCTACCTGAACCAGTGAAGGTGAGCGAACTGCCGGTGCTGATGGGCGAGCGT
TTTGAAGTGCTGGTGGAGGTTAACGATAACAAACCCTTTGACCTGGTGACGCTGCCGGTC
AGCCAGATGGGGATGGCGATTGCGCCGTTTGATAAGCCTCATCCGGTAATGCGGATTCAG
CCGATTGCTATTAGTGCCTCCGGTGCTTTGCCAGACACATTAAGTAGCCTGCCTGCGTTA
CCTTCGCTGGAAGGGCTGACGGTACGCAAGCTGCAACTCTCTATGGACCCGATGCTCGAT
ATGATGGGGATGCAGATGCTAATGGAGAAATATGGCGATCAGGCGATGGCCGGGATGGAT
CACAGCCAGATGATGGGCCATATGGGGCACGGCAATATGAATCATATGAACCACGGCGGG
AAGTTCGATTTCCACCATGCCAACAAAATCAACGGTCAGGCGTTTGATATGAACAAGCCG
ATGTTTGCGGCGGCGAAAGGGCAATACGAACGTTGGGTTATCTCTGGCGTGGGCGACATG
ATGCTGCATCCGTTCCATATCCACGGCACGCAGTTCCGTATCTTGTCAGAAAATGGCAAA
CCGCCAGCGGCTCATCGCGCGGGCTGGAAAGATACCGTTAAGGTAGAAGGTAATGTCAGC
GAAGTGCTGGTGAAGTTTAATCACGATGCACCGAAAGAACATGCTTATATGGCGCACTGC
CATCTGCTGGAGCATGAAGATACGGGGATGATGTTAGGGTTTACGGTATAA
Protein Properties
Pfam Domain Function:
Protein Residues:516
Protein Molecular Weight:56556
Protein Theoretical pI:7
PDB File:1N68
Signaling Regions:
  • 1-28
Transmembrane Regions:
  • None
Protein Sequence:
>Blue copper oxidase cueO
MQRRDFLKYSVALGVASALPLWSRAVFAAERPTLPIPDLLTTDARNRIQLTIGAGQSTFG
GKTATTWGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIP
PGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDDEILKLMLPKQWGIDD
VPVIVQDKKFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCN
ARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGERFEVLVEVNDNKPFDLVTLPV
SQMGMAIAPFDKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTVRKLQLSMDPMLD
MMGMQMLMEKYGDQAMAGMDHSQMMGHMGHGNMNHMNHGGKFDFHHANKINGQAFDMNKP
MFAAAKGQYERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVS
EVLVKFNHDAPKEHAYMAHCHLLEHEDTGMMLGFTV
References
External Links:
ResourceLink
Uniprot ID:P36649
Uniprot Name:CUEO_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674340
PDB ID:1N68
Ecogene ID:EG12318
Ecocyc:EG12318
ColiBase:b0123
Kegg Gene:b0123
EchoBASE ID:EB2223
CCDB:CUEO_ECOLI
BacMap:16128116
General Reference:
  • 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
  • Fountoulakis, M., Takacs, M. F., Berndt, P., Langen, H., Takacs, B. (1999). "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Electrophoresis 20:2181-2195. Pubmed: 10493123
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Grass, G., Rensing, C. (2001). "CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli." Biochem Biophys Res Commun 286:902-908. Pubmed: 11527384
  • Grass, G., Rensing, C. (2001). "Genes involved in copper homeostasis in Escherichia coli." J Bacteriol 183:2145-2147. Pubmed: 11222619
  • 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
  • Kim, C., Lorenz, W. W., Hoopes, J. T., Dean, J. F. (2001). "Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene." J Bacteriol 183:4866-4875. Pubmed: 11466290
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Outten, F. W., Huffman, D. L., Hale, J. A., O'Halloran, T. V. (2001). "The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli." J Biol Chem 276:30670-30677. Pubmed: 11399769
  • Outten, F. W., Outten, C. E., Hale, J., O'Halloran, T. V. (2000). "Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR." J Biol Chem 275:31024-31029. Pubmed: 10915804
  • Roberts, S. A., Weichsel, A., Grass, G., Thakali, K., Hazzard, J. T., Tollin, G., Rensing, C., Montfort, W. R. (2002). "Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli." Proc Natl Acad Sci U S A 99:2766-2771. Pubmed: 11867755
  • Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P., Ribnicky, B., Palmer, T., Georgiou, G. (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282:8309-8316. Pubmed: 17218314