ID A0A2W2GX67_9ACTN Unreviewed; 478 AA.
AC A0A2W2GX67;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C1I98_30085 {ECO:0000313|EMBL:PZG31474.1};
OS Spongiactinospora gelatinilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Spongiactinospora.
OX NCBI_TaxID=2666298 {ECO:0000313|EMBL:PZG31474.1, ECO:0000313|Proteomes:UP000248544};
RN [1] {ECO:0000313|EMBL:PZG31474.1, ECO:0000313|Proteomes:UP000248544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7K107 {ECO:0000313|EMBL:PZG31474.1,
RC ECO:0000313|Proteomes:UP000248544};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Sphaerisporangium sp. 7K107.";
RL Submitted (JAN-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PZG31474.1}.
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DR EMBL; POUA01000325; PZG31474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2GX67; -.
DR Proteomes; UP000248544; 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; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
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; PF00394; Cu-oxidase; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 83..190
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 241..313
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 358..476
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 478 AA; 54205 MW; 639105DF83939824 CRC64;
MHNRLGNHLL NRRNLLALGG LTGAAALLPP GRDGRHGPRP RRLAHVPAFS VEMPLPPVAR
PVQVRPDADV YQVRIKPARV EIVPGLLTPV LSFGGGFVGP TFQVRTGRRV IVKYHNDLDR
AANVHLHGGH VPSVSDGHPM DVIDPGRFRV YDYPNTQQGT TLWYHDHSHH TEARNVYAGL
HGFYVIEDPA EAKYGLPRGR YDVPIMIRDA LIGQDGELIY DVPDTRTTLL ANGRPQPYFR
VAARKYRFRL LNGTTHRLFR LRLEGDLPLI QIGSDGGLLP APQRMRELLI SSGERADVVV
DFSRFKPGDQ VMMHDTSGTV LRFDVVRRAR DHSRVPDVLR PLPDLPEATV TRDVVFNLDL
TTPKWRYLMN EQEFDPARVD FQVRRGATEI WRIHNADVER GGINHTFHLH LEQFRVLDRD
GEPPWPTDLG RKDTIYVPPG ASARIKVRFT EHLGRYVYHC HFLDHSSLGM MAQLQIVP
//
