ASO_CUCMA
ID ASO_CUCMA Reviewed; 579 AA.
AC P24792; Q39539;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 102.
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 Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-48.
RC STRAIN=cv. Ebisu Nankin;
RX PubMed=2143984; DOI=10.1111/j.1432-1033.1990.tb19154.x;
RA Esaka M., Hattori T., Fujisawa K., Sakajo S., Asahi T.;
RT "Molecular cloning and nucleotide sequence of full-length cDNA for
RT ascorbate oxidase from cultured pumpkin cells.";
RL Eur. J. Biochem. 191:537-541(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9210335; DOI=10.1093/oxfordjournals.pcp.a029214;
RA Kisu Y., Harada Y., Goto M., Esaka M.;
RT "Cloning of the pumpkin ascorbate oxidase gene and analysis of a cis-acting
RT region involved in induction by auxin.";
RL Plant Cell Physiol. 38:631-637(1997).
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; X55779; CAA39300.1; -; mRNA.
DR EMBL; D55677; BAA09528.1; -; Genomic_DNA.
DR PIR; S11027; S11027.
DR AlphaFoldDB; P24792; -.
DR SMR; P24792; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000504608; 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 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; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:2143984"
FT CHAIN 31..579
FT /note="L-ascorbate oxidase"
FT /id="PRO_0000002907"
FT DOMAIN 33..152
FT /note="Plastocyanin-like 1"
FT DOMAIN 164..330
FT /note="Plastocyanin-like 2"
FT DOMAIN 374..553
FT /note="Plastocyanin-like 3"
FT BINDING 90
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 92
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 134
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 136
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 475
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 478
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 480
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 536
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 537
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 538
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 542
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 547
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 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..231
FT /evidence="ECO:0000250"
FT DISULFID 111..568
FT /evidence="ECO:0000250"
FT DISULFID 210..223
FT /evidence="ECO:0000250"
FT CONFLICT 175
FT /note="W -> C (in Ref. 1; CAA39300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 64668 MW; 8F5AF4CB07B276B9 CRC64;
MLQMGKAREP NFLILFFFGL ILAFGISSEG SQIRHYKWEV EYMFWAPDCN ENIVMGINGQ
FPGPTIRANA GDTVVVELIN KLHTEGVVIH WHGILQRGTP WADGTASISQ CAINPGETFF
YNFTVDNPGT FFYHGHLGMQ RSAGLYGSLI VDPPQGKKEP FHYDGEINLL LSDWWHQSIH
KQEVGLSSKP IRWIGEPQTI LLNGRGQFDC SIAAKYDSNL EPCKLKGSEP CAPYIFHVMP
KKTYRIRIAS TTALAALNFA IGNHPLLVVE ADGNYVQPFY TSDIDIYSGE SYSVLITTDQ
NPSENYWVSV GTRGRHPNTP PGLTLLNYLP NSVSKLPTSP PPETPAWDDF DRSKNFTYRI
TAAMGSPKPP VKSNRRIFLL NTQNVINGYV KWAINDVSLA LPPTPYLGAM KFNLLHAFDQ
NPPPEVFPED YDIDTPPTNE KTKIGNGVYQ FKIGEIVDVI LQNANMMKEN LSEIHPWHLH
GHDFWVLGYG DGKFTAEEES SLNLKNPPLR NTVVIFPYGW TAIRFVADNP GVWAFHCHIE
PHLHMGMGVV FAEGVEKVGR IPTKALACGG TAKSLINNP
