ASO_TOBAC
ID ASO_TOBAC Reviewed; 578 AA.
AC Q40588;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=L-ascorbate oxidase;
DE Short=ASO;
DE Short=Ascorbase;
DE EC=1.10.3.3;
DE Flags: Precursor;
GN Name=AAO;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8624413; DOI=10.1007/bf00019015;
RA Kato N., Esaka M.;
RT "cDNA cloning and gene expression of ascorbate oxidase in tobacco.";
RL Plant Mol. Biol. 30:833-837(1996).
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 -!- TISSUE SPECIFICITY: Highly expressed in young and growing tissues.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; D43624; BAA07734.1; -; mRNA.
DR PIR; S66353; S66353.
DR RefSeq; NP_001313101.1; NM_001326172.1.
DR AlphaFoldDB; Q40588; -.
DR SMR; Q40588; -.
DR STRING; 4097.Q40588; -.
DR GeneID; 107826841; -.
DR KEGG; nta:107826841; -.
DR BRENDA; 1.10.3.3; 3645.
DR Proteomes; UP000084051; Unplaced.
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 GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..578
FT /note="L-ascorbate oxidase"
FT /id="PRO_0000002908"
FT DOMAIN 30..149
FT /note="Plastocyanin-like 1"
FT DOMAIN 161..328
FT /note="Plastocyanin-like 2"
FT DOMAIN 372..550
FT /note="Plastocyanin-like 3"
FT BINDING 87
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 89
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 131
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 133
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 472
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 475
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 477
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 533
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 534
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 535
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 539
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="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..565
FT /evidence="ECO:0000250"
FT DISULFID 207..221
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 64865 MW; C2371F5FEA353E3B CRC64;
MASLGFLFFF LLPLILLELS SSRSVMAAKT RHFKWDVEYI HWSPDGEESV VMGINGQFPG
PTIRAKAGDT VAVHLTNKLH TEGVVIHWHG IRQIGTPWAD GTAAISQCAI NPGETFLYRF
KVDKAGTYFY HGHYGMQRSA GLYGSLIVEV GEGEKEPFHY DGEFNLLLSD WWHKGSHEQE
VDLSSNPLRW IGEPQTLLLN GRGQYNCSLA ARFSKPPLPQ CKLRGGEQYA PQILRVRPNK
IYRLRVASTT ALGSLSLAIG GHKMVVVEAD GNYVQPFSVQ DMDIYSGESY SVLFKTDQDP
TKNYWISINV RGREPKTPQG LTLLNYLPNS ASKFPTLPPP IAPLWNDYNH SKSFSNKIFA
LMGSPKPPPQ NHRRIILLNT QNKIDGYTKW AINNVSLVLP TQLYLGSIRY GINAFDTKPP
PDNFPKDYDV LKQAPNSNST YGNGVYMLKF NTTIDIILQN ANALAKDVSE IHPWHLHGHD
FWVLGYGEGK FSEKDVKKFN LKNPPLRNTA VIFPFGWTAL RFVTDNPGVW AFHCHIEPHL
HMGMGVIFAE GVHLVKKIPK EALACGLTGK MLMSNKHN
