GenomeNet

Database: UniProt
Entry: A0A1R3K1Y0_9ROSI
LinkDB: A0A1R3K1Y0_9ROSI
Original site: A0A1R3K1Y0_9ROSI 
ID   A0A1R3K1Y0_9ROSI        Unreviewed;       572 AA.
AC   A0A1R3K1Y0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=L-ascorbate oxidase {ECO:0000256|ARBA:ARBA00022095};
DE            EC=1.10.3.3 {ECO:0000256|ARBA:ARBA00012301};
GN   ORFNames=COLO4_12155 {ECO:0000313|EMBL:OMP01100.1};
OS   Corchorus olitorius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=93759 {ECO:0000313|EMBL:OMP01100.1, ECO:0000313|Proteomes:UP000187203};
RN   [1] {ECO:0000313|Proteomes:UP000187203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA   Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA   Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA   Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA   Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA   Shommy N.S.;
RT   "Corchorus olitorius genome sequencing.";
RL   Submitted (SEP-2013) 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   -!- 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:OMP01100.1}.
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; AWUE01014840; OMP01100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3K1Y0; -.
DR   STRING; 93759.A0A1R3K1Y0; -.
DR   OrthoDB; 449862at2759; -.
DR   Proteomes; UP000187203; 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:SF237; L-ASCORBATE OXIDASE; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187203};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..572
FT                   /note="L-ascorbate oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013385879"
FT   DOMAIN          38..150
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          167..321
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          423..548
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   572 AA;  63718 MW;  40E89D6F58B9742F CRC64;
     MVGILRILSF ILLLTCIFVS LSVGLAAAAR DRKFTWEISY QHKSLDCYKK LAVAINGLTP
     GPTISAEQGD RIIVNVTNNL FMENVAIHWH GIRQRGTPWS DGTDGVSQCA IMPGETYTYE
     FVVDRAGTFM YHSHYGLQRE AGLYGLITVS LPVGVSEPFS YDFDREIILS DWYHNTTYET
     ATDLASIPFL WVGEPQSLLI NGRGNYSCSG LAASVCNSTN PECLPSNLTV ISGKTYRLRI
     ASLTSLSALS FQIEDHEMTV VEADGHYVEP FVVNNLYIYS GETYSVLVTA NQNSSRNYWT
     TINVVSRQPN TPNGIAIFNY DPIDYQKLPP TNPPPGPLWN DTKSQVNQSR AIKARQGFIV
     TPPKKPDRVI VLLNTQNTID GYVRWSLNNV SHTLPSTPLL IAIKENMTGV FDPNPPPDDN
     DSANYDIYSV ANNTNSVSSS SIYRLQFNST VDIILQNANT MTANVSESHP WHLHGHDFWV
     LGYGEGKFNL SRDTETYNLA DPIMKNTVPL HPYGWTALRF KADNPGVWLF HCHIEAHFFL
     GMLVVFESGV EQVGDIPLSN YGCGQTKSFI KP
//
DBGET integrated database retrieval system