ASO_CUCSA
ID ASO_CUCSA Reviewed; 587 AA.
AC P14133;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=L-ascorbate oxidase;
DE Short=ASO;
DE Short=Ascorbase;
DE EC=1.10.3.3;
DE Flags: Precursor;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-58.
RX PubMed=2919172; DOI=10.1073/pnas.86.4.1239;
RA Ohkawa J., Okada N., Shinmyo A., Takano M.;
RT "Primary structure of cucumber (Cucumis sativus) ascorbate oxidase deduced
RT from cDNA sequence: homology with blue copper proteins and tissue-specific
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1239-1243(1989).
CC -!- FUNCTION: May be involved in a redox system involving ascorbic acid.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; J04494; AAA33119.1; -; mRNA.
DR PIR; A30094; KSKVAO.
DR RefSeq; XP_004149015.1; XM_004148967.2.
DR AlphaFoldDB; P14133; -.
DR SMR; P14133; -.
DR STRING; 3659.XP_004168020.1; -.
DR EnsemblPlants; KGN66418; KGN66418; Csa_1G604040.
DR GeneID; 101215231; -.
DR Gramene; KGN66418; KGN66418; Csa_1G604040.
DR KEGG; csv:101215231; -.
DR eggNOG; KOG1263; Eukaryota.
DR OMA; VHYDDTM; -.
DR BRENDA; 1.10.3.3; 1733.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008447; F:L-ascorbate oxidase activity; IEA:UniProtKB-EC.
DR CDD; cd13845; CuRO_1_AAO; 1.
DR CDD; cd13893; CuRO_3_AAO; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034259; CuRO_1_AAO.
DR InterPro; IPR034267; CuRO_3_AAO.
DR InterPro; IPR017760; L-ascorbate_oxidase_pln.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR TIGRFAMs; TIGR03388; ascorbase; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:2919172"
FT CHAIN 34..587
FT /note="L-ascorbate oxidase"
FT /id="PRO_0000002906"
FT DOMAIN 38..157
FT /note="Plastocyanin-like 1"
FT DOMAIN 169..335
FT /note="Plastocyanin-like 2"
FT DOMAIN 379..559
FT /note="Plastocyanin-like 3"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..236
FT /evidence="ECO:0000250"
FT DISULFID 116..574
FT /evidence="ECO:0000250"
FT DISULFID 215..228
FT /evidence="ECO:0000250"
SQ SEQUENCE 587 AA; 65876 MW; A192DB7405150074 CRC64;
MAKVADKPFF PKPFLSFLVL SIIFGFGITL SEAGFPKIKH YKWDVEYMFW SPDCVENIVM
GINGEFPGPT IRANAGDIVV VELTNKLHTE GVVIHWHGIL QRGTPWADGT ASISQCAINP
GETFTYRFVV DKAGTYFYHG HLGMQRSAGL YGSLIVDPPE GRSEPFHYDE EINLLLSDWW
HQSVHKQEVG LSSKPMRWIG EPQSILINGK GQFDCSIAAK YNQGLKQCEL SGKEKCAPFI
LHVQPKKTYR IRIASTTALA SLNFAIGNHE LLVVEADGNY VQPFVTSDID IYSGESYSVL
ITTDQNPLEN YWVSIGVRAR LPKTPPGLTL LNYLPNSASK LPISPPPETP HWEDFDRSKN
FTFRIFAAMG SPKPPVRYNR RLFLLNTQNR INGFMKWAIN NVSLALPPTP YLAAMKMRLN
TAFNQNPPPE TFPLNYDINN PPPNPETTTG NGVYKFNMGE TVDVILQNAN MLNPNMSEIH
PWHLHGHDFW VLGYGEGKFY APEDEKKLNL KNPPLRNTVV IFPYGWTAIR FVADNPGVWA
FHCHIEPHLH MGMGVVFAEG VHMVGMIPPK ALACGSTALV KNYPRLP
