ID A0A1S4D7M9_TOBAC Unreviewed; 578 AA.
AC A0A1S4D7M9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=L-ascorbate oxidase {ECO:0000256|ARBA:ARBA00022095};
DE EC=1.10.3.3 {ECO:0000256|ARBA:ARBA00012301};
GN Name=LOC107826841 {ECO:0000313|RefSeq:XP_016509366.1};
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 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016509366.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016509366.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_016509366.1; XM_016653880.1.
DR AlphaFoldDB; A0A1S4D7M9; -.
DR GeneID; 107826841; -.
DR OMA; VDWYHVA; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; cd13845; CuRO_1_AAO; 1.
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; IPR034259; CuRO_1_AAO.
DR InterPro; IPR034267; CuRO_3_AAO.
DR InterPro; IPR017760; L-ascorbate_oxidase_pln.
DR NCBIfam; TIGR03388; ascorbase; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF394; PLASTOCYANIN-LIKE DOMAIN-CONTAINING PROTEIN; 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:UP000084051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..578
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010299389"
FT DOMAIN 37..149
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 164..327
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 436..551
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 578 AA; 64822 MW; 4E24AD05DFFAD78C 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 ALASLSLAIG GHKMVVVEAD GNYVQPFSVQ DMDIYSGESY SVLFKTDQDP
TKNYWISINV RGREPKTPQG LTLLNYLPNS ASKFPTLPPP IAPLWNDYNH SKSFSNKIFA
LMGSPKPPPQ NHRRIILLNT QNKIDGYTKW AINNVSLVLP TTPYLGSIRY GINAFDTKPP
PDNFPKDYDV LKQAPNSNST YGNGVYMLKF NTTIDIILQN ANALAKDVSE IHPWHLHGHD
FWVLGYGEGK FSEKDVKKFN LKNPPLRNTA VIFPFGWTAL RFVTDNPGVW AFHCHIEPHL
HMGMGVVFAE GVHLVKKIPK EALACGLTGK MLMSNKHN
//
