ID A0A1H6ETD2_9ACTN Unreviewed; 546 AA.
AC A0A1H6ETD2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Multicopper oxidase CueO {ECO:0000256|ARBA:ARBA00041027};
DE EC=1.16.3.4 {ECO:0000256|ARBA:ARBA00038978};
DE AltName: Full=Copper efflux oxidase {ECO:0000256|ARBA:ARBA00042896};
DE AltName: Full=Cuprous oxidase {ECO:0000256|ARBA:ARBA00043090};
GN ORFNames=SAMN05444920_11948 {ECO:0000313|EMBL:SEH01118.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEH01118.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEH01118.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEH01118.1,
RC ECO:0000313|Proteomes:UP000236732};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Cu(+) + 4 H(+) + O2 = 4 Cu(2+) + 2 H2O;
CC Xref=Rhea:RHEA:30083, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552; EC=1.16.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30084;
CC Evidence={ECO:0000256|ARBA:ARBA00036588};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR EMBL; FNVT01000019; SEH01118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ETD2; -.
DR OrthoDB; 345021at2; -.
DR Proteomes; UP000236732; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 4.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Capsid protein {ECO:0000313|EMBL:SEH01118.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000236732};
KW Virion {ECO:0000313|EMBL:SEH01118.1}.
FT DOMAIN 104..237
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 441..545
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 59055 MW; 30FD6020CC24121A CRC64;
MPGQTGDVPG PTGIPPGPTG DVPGPTGVLS RRAFLGLAGG AGVVLAAGLA GPRLLSAGAQ
GTGELLRSGI PLPEPFRVPL PIPRVLRPYT KDGTDRYTIT QREATAEIIP GVRTPIWGYD
GTFPGPTIES RRDRTAVIHH RNELPVPTVV HLHGGRTPAD SDGYPTDLVL PAAGWDDGHS
GHGMHDARAR IAQGSRDYLF PMRQRAATLW YHDHRMDFTG PAVYRGLAGF HLIRDDEEEA
LDLPAGDREL PLMIADRAFD EHGAFAYPSL DPTLRTTPGV TEAYVEGVFG DVILVNGAPW
PIHEVAAARY RLRVLNASNA RRYDLALDPP PPGGGGFVQI GSDLGLLDAP RSHDHLPIGP
AERYDVVVDF GRYPVGAQVT LVNRLGTGPT ARVMRFVVAR RAPDESRIPP KLSDLAPPSR
SQATTVREFA FRGGHVHGRA GWVIGGEPFA PDRMSARPRL GDVEIWRFVA DVHHPVHLHL
VGFHILSRGG RPPGPFDGGL KDTVDLSPGQ SVEVIARFDG YRGRYVFHCH NAEHEDMAMM
ANFEVI
//