1.B.76.1.8
Blue multi-copper oxidase of 516 aas, CueO. CueO is involved in
copper tolerance under aerobic conditions. It features the four typical
copper atoms that act as electron transfer (T1) and dioxygen reduction
(T2, T3; trinuclear) sites. In addition, it displays a methionine- and
histidine-rich insert that includes a helix that blocks physical access
to the T1 site (Cortes et al. 2015). It catalyzes oxidation of Mn2+ (Su et al. 2014). Also referred to as copper efflux oxidase (Kataoka et al. 2013).
|
| Accession Number: | P36649 |
|---|
| Protein Name: | Blue copper oxidase CueO |
|---|
| Length: | 516 |
|---|
| Molecular Weight: | 56556.00 |
|---|
| Species: | Escherichia coli (strain K12) [83333] |
|---|
| Number of TMSs: | 1 |
|---|
| Location1 / Topology2 / Orientation3: |
Periplasm1 |
|---|
| Substrate |
copper(2+) |
|---|
1: MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG
61: GKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP
121: PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD
181: VPVIVQDKKF SADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN
241: ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV
301: SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD
361: MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP
421: MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS
481: EVLVKFNHDA PKEHAYMAHC HLLEHEDTGM MLGFTV