Entry
Name
cuproxidase;
cueO (gene name);
cuprous oxidase;
Cu(I) oxidase;
copper efflux oxidase
Class
Oxidoreductases;
Oxidizing metal ions;
With oxygen as acceptor
BRITE hierarchy
Sysname
copper(I):oxygen oxidoreductase
Reaction(IUBMB)
4 Cu+ + 4 H+ + O2 = 4 Cu2+ + 2 H2O [RN:
R12925 ]
Reaction(KEGG)
Substrate
Product
Comment
The enzyme, characterized from the bacterium Escherichia coli, is involved in copper tolerance under aerobic conditions. The enzyme contains a substrate binding (type 1) copper site and a trinuclear copper center (consisting of type 2 and type 3 copper sites) in which oxygen binding and reduction takes place. It also contains a methionine rich region that can bind additional copper ions. In vitro, if the substrate binding site is occupied by copper(II), the enzyme can function as a laccase-type quinol oxidase (EC
1.10.3.2 ). However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.
History
EC 1.16.3.4 created 2021
Orthology
Genes
ECOO : ECRM13514_0125(yacK)
ECOH : ECRM13516_0128(yacK)
ECW : EcE24377A_0125(cueO)
EDJ : ECDH1ME8569_0117(cueO)
ECOI : ECOPMV1_00129(cueO)
REE : electrica_04206(cueO)
RTG : NCTC13098_06152(cueO_3)
CLAP : NCTC11466_03798(cueO)
KIE : NCTC12125_02910(cueO)
AHN : NCTC12129_00920(cueO)
METY : MRY16398_46930(cueO)
PSHI : SAMEA2665130_0426(cueO)
YPG : YpAngola_A1021(cueO)
YPI : YpsIP31758_3352(cueO)
YCA : F0T03_02120(cueO) F0T03_04145(cueO)
YKI : HRD70_06535(cueO) HRD70_08460(cueO)
SMW : SMWW4_v1c41080(cueO)
SFJ : SAMEA4384070_4119(cueO)
SOF : NCTC11214_02620(cueO_1)
SSAR : SSARUM_004000(cueO)
RIU : I2123_03925(cueO) I2123_20025(cueO)
DIC : Dpoa569_002062(cueO)
TPTY : NCTC11468_03055(cueO)
PHEI : NCTC12003_01021(cueO)
PRJ : NCTC6933_03024(cueO)
ANS : ArsFIN_36830(cueO_2)
» show all
Taxonomy
Reference
Authors
Kim C, Lorenz WW, Hoopes JT, Dean JF
Title
Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene.
Journal
Reference
Authors
Grass G, Rensing C.
Title
CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli.
Journal
Sequence
Reference
Authors
Outten FW, Huffman DL, Hale JA, O'Halloran TV
Title
The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli.
Journal
Reference
Authors
Roberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR.
Title
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli.
Journal
Sequence
Reference
Authors
Roberts SA, Wildner GF, Grass G, Weichsel A, Ambrus A, Rensing C, Montfort WR.
Title
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO.
Journal
Sequence
Reference
Authors
Singh SK, Grass G, Rensing C, Montfort WR.
Title
Cuprous oxidase activity of CueO from Escherichia coli.
Journal
Reference
Authors
Galli I, Musci G, Bonaccorsi di Patti MC.
Title
Sequential reconstitution of copper sites in the multicopper oxidase CueO.
Journal
Reference
Authors
Djoko KY, Chong LX, Wedd AG, Xiao Z.
Title
Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase.
Journal
Sequence
Reference
Authors
Singh SK, Roberts SA, McDevitt SF, Weichsel A, Wildner GF, Grass GB, Rensing C, Montfort WR.
Title
Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence.
Journal
Sequence
Reference
Authors
Cortes L, Wedd AG, Xiao Z.
Title
The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.16.3.4
ExPASy - ENZYME nomenclature database: 1.16.3.4