ID A0A0E0QQG1_ORYRU Unreviewed; 577 AA.
AC A0A0E0QQG1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=L-ascorbate oxidase {ECO:0000256|ARBA:ARBA00022095};
DE EC=1.10.3.3 {ECO:0000256|ARBA:ARBA00012301};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI09G08140.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI09G08140.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0E0QQG1; -.
DR SMR; A0A0E0QQG1; -.
DR STRING; 4529.A0A0E0QQG1; -.
DR EnsemblPlants; ORUFI09G08140.1; ORUFI09G08140.1; ORUFI09G08140.
DR Gramene; ORUFI09G08140.1; ORUFI09G08140.1; ORUFI09G08140.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_8_3_1; -.
DR OMA; RGYEQCE; -.
DR Proteomes; UP000008022; 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:UP000008022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..577
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002371624"
FT DOMAIN 34..145
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 164..325
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 424..556
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 62872 MW; D77B4BC83A88DD51 CRC64;
MMRCSDRLLC SLFLAAALFG VAAAATRRHD WDISYQFTSP DCVRKLAVTI NGHTPGPTIR
AVQGDTIVVN VKNSLLTENV AIHWHGIRQI GTPWADGTEG VTQCPILPGD TFAYTFVVDR
PGTYMYHAHY GMQRSAGLNG MIVVEVAPGA AGDGEREPFR YDGEHTVLLN DWWHRSTYEQ
AAGLASVPMV WVGEPQSLLI NGRGRFVNCS SSPATAASCN VSHPDCAPAV FAVVPGKTYR
FRVASVTSLS ALNFEIEGHE MTVVEADGHY VKPFVVKNLN IYSGETYSVL ITADQDPNRN
YWLASNVVSR KPATPTGTAV LAYYGGRRNS PRARPPTPPP AGPAWNDTAY RVRQSLATVA
HPAHAVPPPP TSDRTILLLN TQNKIGGQIK WALNNVSFTL PHTPYLVAMK RGLLGAFDQR
PPPETYAGAA AFDVYAVQGN PNATTSDAPY RLRFGSVVDV VLQNANMLAA NSSETHPWHL
HGHDFWVLGH GAGRFDPAVH PAAYNLRDPI MKNTVAVHPF GWTALRFRAD NPGVWAFHCH
IEAHFFMGMG IVFEEGVERV GELPPEIMGC GKTRGGH
//