ASO_CUCPM
ID ASO_CUCPM Reviewed; 552 AA.
AC P37064;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=L-ascorbate oxidase;
DE Short=ASO;
DE Short=Ascorbase;
DE EC=1.10.3.3;
OS Cucurbita pepo var. melopepo (Zucchini).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3665;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT
RP ASN-92, SUBUNIT, AND METAL BINDING.
RX PubMed=1548698; DOI=10.1016/0022-2836(92)90583-6;
RA Messerschmidt A., Ladenstein R., Huber R., Bolognesi M., Avigliano L.,
RA Petruzzelli R., Rossi A., Finazzi-Agro A.;
RT "Refined crystal structure of ascorbate oxidase at 1.9-A resolution.";
RL J. Mol. Biol. 224:179-205(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND METAL BINDING.
RX PubMed=2716059; DOI=10.1016/0022-2836(89)90498-1;
RA Messerschmidt A., Rossi A., Ladenstein R., Huber R., Bolognesi M.,
RA Gatti G., Marchesini A., Petruzzelli R., Finazzi-Agro A.;
RT "X-ray crystal structure of the blue oxidase ascorbate oxidase from
RT zucchini. Analysis of the polypeptide fold and a model of the copper sites
RT and ligands.";
RL J. Mol. Biol. 206:513-529(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;
CC Note=Binds 4 Cu cations per monomer. The Cu cations are bound as 3
CC distinct Cu centers known as type 1 or blue, type 2 or normal, and type
CC 3 or coupled binuclear.;
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:1548698}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR PIR; A51027; A51027.
DR PDB; 1AOZ; X-ray; 1.90 A; A/B=1-552.
DR PDB; 1ASO; X-ray; 2.20 A; A/B=1-552.
DR PDB; 1ASP; X-ray; 2.59 A; A/B=1-552.
DR PDB; 1ASQ; X-ray; 2.32 A; A/B=1-552.
DR PDBsum; 1AOZ; -.
DR PDBsum; 1ASO; -.
DR PDBsum; 1ASP; -.
DR PDBsum; 1ASQ; -.
DR AlphaFoldDB; P37064; -.
DR SMR; P37064; -.
DR GlyConnect; 328; 4 N-Linked glycans (1 site).
DR BioCyc; MetaCyc:MON-17019; -.
DR BRENDA; 1.10.3.3; 1740.
DR EvolutionaryTrace; P37064; -.
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; cd13871; CuRO_2_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; IPR034258; CuRO_2_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 3D-structure; Copper; Disulfide bond; Glycoprotein; Metal-binding;
KW Oxidoreductase; Repeat; Secreted.
FT CHAIN 1..552
FT /note="L-ascorbate oxidase"
FT /id="PRO_0000085582"
FT DOMAIN 1..122
FT /note="Plastocyanin-like 1"
FT DOMAIN 134..300
FT /note="Plastocyanin-like 2"
FT DOMAIN 344..523
FT /note="Plastocyanin-like 3"
FT BINDING 60
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 104
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 445
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 448
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 450
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 506
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 507
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 508
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 512
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT BINDING 517
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:1548698"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1548698"
FT /id="CAR_000149"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 19..201
FT /evidence="ECO:0000269|PubMed:1548698"
FT DISULFID 81..538
FT /evidence="ECO:0000269|PubMed:1548698"
FT DISULFID 180..193
FT /evidence="ECO:0000269|PubMed:1548698"
FT STRAND 3..15
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1AOZ"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1AOZ"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 344..356
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 454..463
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 466..471
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 489..496
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 510..514
FT /evidence="ECO:0007829|PDB:1AOZ"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:1AOZ"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:1AOZ"
SQ SEQUENCE 552 AA; 61704 MW; 24660B0F47AB54B4 CRC64;
SQIRHYKWEV EYMFWAPNCN ENIVMGINGQ FPGPTIRANA GDSVVVELTN KLHTEGVVIH
WHGILQRGTP WADGTASISQ CAINPGETFF YNFTVDNPGT FFYHGHLGMQ RSAGLYGSLI
VDPPQGKKEP FHYDGEINLL LSDWWHQSIH KQEVGLSSKP IRWIGEPQTI LLNGRGQFDC
SIAAKYDSNL EPCKLKGSES CAPYIFHVSP KKTYRIRIAS TTALAALNFA IGNHQLLVVE
ADGNYVQPFY TSDIDIYSGE SYSVLITTDQ NPSENYWVSV GTRARHPNTP PGLTLLNYLP
NSVSKLPTSP PPQTPAWDDF DRSKNFTYRI TAAMGSPKPP VKFNRRIFLL NTQNVINGYV
KWAINDVSLA LPPTPYLGAM KYNLLHAFDQ NPPPEVFPED YDIDTPPTNE KTRIGNGVYQ
FKIGEVVDVI LQNANMMKEN LSETHPWHLH GHDFWVLGYG DGKFSAEEES SLNLKNPPLR
NTVVIFPYGW TAIRFVADNP GVWAFHCHIE PHLHMGMGVV FAEGVEKVGR IPTKALACGG
TAKSLINNPK NP
