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P37064 (ASO_CUCPM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-ascorbate oxidase
Short name=ASO
Short name=Ascorbase
EC=1.10.3.3
OrganismCucurbita pepo var. melopepo (Zucchini)
Taxonomic identifier3665 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucurbiteae › Cucurbita ›

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in a redox system involving ascorbic acid.

Catalytic activity

4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O.

Cofactor

Binds 4 copper ions per monomer. The copper ions are bound as 3 distinct copper centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.

Subunit structure

Dimer. Ref.1

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-ascorbate oxidase activity

Inferred from electronic annotation. Source: EC

copper ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552L-ascorbate oxidase
PRO_0000085582

Regions

Domain1 – 122122Plastocyanin-like 1
Domain134 – 300167Plastocyanin-like 2
Domain344 – 523180Plastocyanin-like 3

Sites

Metal binding601Copper 1; type 2 Ref.1
Metal binding621Copper 2; type 3 Ref.1
Metal binding1041Copper 2; type 3 Ref.1
Metal binding1061Copper 3; type 3 Ref.1
Metal binding4451Copper 4; type 1 Ref.1
Metal binding4481Copper 1; type 2 Ref.1
Metal binding4501Copper 3; type 3 Ref.1
Metal binding5061Copper 3; type 3 Ref.1
Metal binding5071Copper 4; type 1 Ref.1
Metal binding5081Copper 2; type 3 Ref.1
Metal binding5121Copper 4; type 1 Ref.1
Metal binding5171Copper 4; type 1 Ref.1

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Ref.1
CAR_000149
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Disulfide bond19 ↔ 201 Ref.1
Disulfide bond81 ↔ 538 Ref.1
Disulfide bond180 ↔ 193 Ref.1

Secondary structure

1 ............................................................................................. 552
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37064 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 24660B0F47AB54B4

FASTA55261,704
        10         20         30         40         50         60 
SQIRHYKWEV EYMFWAPNCN ENIVMGINGQ FPGPTIRANA GDSVVVELTN KLHTEGVVIH 

        70         80         90        100        110        120 
WHGILQRGTP WADGTASISQ CAINPGETFF YNFTVDNPGT FFYHGHLGMQ RSAGLYGSLI 

       130        140        150        160        170        180 
VDPPQGKKEP FHYDGEINLL LSDWWHQSIH KQEVGLSSKP IRWIGEPQTI LLNGRGQFDC 

       190        200        210        220        230        240 
SIAAKYDSNL EPCKLKGSES CAPYIFHVSP KKTYRIRIAS TTALAALNFA IGNHQLLVVE 

       250        260        270        280        290        300 
ADGNYVQPFY TSDIDIYSGE SYSVLITTDQ NPSENYWVSV GTRARHPNTP PGLTLLNYLP 

       310        320        330        340        350        360 
NSVSKLPTSP PPQTPAWDDF DRSKNFTYRI TAAMGSPKPP VKFNRRIFLL NTQNVINGYV 

       370        380        390        400        410        420 
KWAINDVSLA LPPTPYLGAM KYNLLHAFDQ NPPPEVFPED YDIDTPPTNE KTRIGNGVYQ 

       430        440        450        460        470        480 
FKIGEVVDVI LQNANMMKEN LSETHPWHLH GHDFWVLGYG DGKFSAEEES SLNLKNPPLR 

       490        500        510        520        530        540 
NTVVIFPYGW TAIRFVADNP GVWAFHCHIE PHLHMGMGVV FAEGVEKVGR IPTKALACGG 

       550 
TAKSLINNPK NP

« Hide

References

[1]"Refined crystal structure of ascorbate oxidase at 1.9-A resolution."
Messerschmidt A., Ladenstein R., Huber R., Bolognesi M., Avigliano L., Petruzzelli R., Rossi A., Finazzi-Agro A.
J. Mol. Biol. 224:179-205(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-92, SUBUNIT, METAL BINDING.
[2]"X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands."
Messerschmidt A., Rossi A., Ladenstein R., Huber R., Bolognesi M., Gatti G., Marchesini A., Petruzzelli R., Finazzi-Agro A.
J. Mol. Biol. 206:513-529(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), METAL BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA51027.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOZX-ray1.90A/B1-552[»]
1ASOX-ray2.20A/B1-552[»]
1ASPX-ray2.59A/B1-552[»]
1ASQX-ray2.32A/B1-552[»]
ProteinModelPortalP37064.
SMRP37064. Positions 1-552.
ModBaseSearch...

PTM databases

GlycoSuiteDBP37064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17019.

Family and domain databases

Gene3D2.60.40.420. 3 hits.
InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR017760. L-ascorbate_oxidase_pln.
[Graphical view]
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 3 hits.
TIGRFAMsTIGR03388. ascorbase. 1 hit.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37064.

Entry information

Entry nameASO_CUCPM
AccessionPrimary (citable) accession number: P37064
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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