ID   A0A2G5DX43_AQUCA        Unreviewed;       552 AA.
AC   A0A2G5DX43;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=L-ascorbate oxidase {ECO:0000256|ARBA:ARBA00022095};
DE            EC=1.10.3.3 {ECO:0000256|ARBA:ARBA00012301};
GN   ORFNames=AQUCO_01400555v1 {ECO:0000313|EMBL:PIA48045.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA48045.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA48045.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate
CC         radical; Xref=Rhea:RHEA:30243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=1.10.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000516};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- SUBUNIT: Dimer. {ECO:0000256|ARBA:ARBA00011473}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ305031; PIA48045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5DX43; -.
DR   STRING; 218851.A0A2G5DX43; -.
DR   InParanoid; A0A2G5DX43; -.
DR   OrthoDB; 449862at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008447; F:L-ascorbate oxidase activity; IEA:UniProtKB-EC.
DR   CDD; cd13893; CuRO_3_AAO; 1.
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; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034267; CuRO_3_AAO.
DR   InterPro; IPR017760; L-ascorbate_oxidase_pln.
DR   NCBIfam; TIGR03388; ascorbase; 1.
DR   PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 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; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          16..128
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          144..305
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          406..532
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   552 AA;  62336 MW;  3A4BDEDD9B24299C CRC64;
     MAQTAEARVR RYKWEVKYEY RSPDCFKKLV IAINGRTPGP SIIAKQGDTI IVELKNSLLT
     ENVAIHWHGI RQIGTPWSDG TEGVSQCPIL PGDTFTYMFV VDRPGTYLYH AHYGMQREAG
     LYGSIRVAVP DGVTEPFSYD YDRSIILNDW YHRSAYEQAT RLSSRPFQWV GEPQSLLIQG
     KGRFNCSSLT TPSLEPGVCN TTTPECSPYV ITVVPGKTYR LRISSLTSLS ALNFEIEGHN
     LTVVEADGHY VEPFVVKNIH IYSGETYSVL VKADQDPSRN YWAASNIVSR EPVTPTGLAI
     LNYYPNHPRK LPPTTPPTGP LWNDTESRFA QAVAIKSHKG YIHPPPLTSD RVIILLNTQN
     EIDGFRRWSV NNVSFTLPHT PYLIALKERK GHLFDQKPPP ENYDVANYDI YKVQENRNAT
     SSNGIYRLKF NSTVDIILQN ANTMNPKNSE THPWHLHGHD FWVMGHGKGK FDPINDPKKY
     NLVDPIMKNT VSVQPYGWTA LRFVADNPGV WAFHCHIEAH FYMGMGVVFE EGVEKVGQLP
     SSIKGCGETR AH
//