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Protein

L-ascorbate oxidase

Gene
N/A
Organism
Cucurbita pepo var. melopepo (Zucchini)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in a redox system involving ascorbic acid.

Catalytic activityi

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

Cofactori

Cu cationNote: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Copper 1; type 21 Publication
Metal bindingi62 – 621Copper 2; type 31 Publication
Metal bindingi104 – 1041Copper 2; type 31 Publication
Metal bindingi106 – 1061Copper 3; type 31 Publication
Metal bindingi445 – 4451Copper 4; type 11 Publication
Metal bindingi448 – 4481Copper 1; type 21 Publication
Metal bindingi450 – 4501Copper 3; type 31 Publication
Metal bindingi506 – 5061Copper 3; type 31 Publication
Metal bindingi507 – 5071Copper 4; type 11 Publication
Metal bindingi508 – 5081Copper 2; type 31 Publication
Metal bindingi512 – 5121Copper 4; type 11 Publication
Metal bindingi517 – 5171Copper 4; type 11 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17019.
BRENDAi1.10.3.3. 1740.

Names & Taxonomyi

Protein namesi
Recommended name:
L-ascorbate oxidase (EC:1.10.3.3)
Short name:
ASO
Short name:
Ascorbase
OrganismiCucurbita pepo var. melopepo (Zucchini)
Taxonomic identifieri3665 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552L-ascorbate oxidasePRO_0000085582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi19 ↔ 2011 Publication
Disulfide bondi81 ↔ 5381 Publication
Glycosylationi92 – 921N-linked (GlcNAc...)1 PublicationCAR_000149
Disulfide bondi180 ↔ 1931 Publication
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP37064.

Interactioni

Subunit structurei

Dimer.1 Publication

Structurei

Secondary structure

1
552
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1513Combined sources
Beta strandi22 – 276Combined sources
Beta strandi30 – 323Combined sources
Beta strandi36 – 394Combined sources
Beta strandi43 – 508Combined sources
Beta strandi59 – 624Combined sources
Helixi70 – 723Combined sources
Turni76 – 783Combined sources
Beta strandi88 – 947Combined sources
Beta strandi99 – 1057Combined sources
Turni108 – 1103Combined sources
Helixi111 – 1133Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi134 – 14411Combined sources
Helixi149 – 1557Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi178 – 1814Combined sources
Helixi184 – 1863Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi213 – 2208Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi244 – 2529Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi261 – 2677Combined sources
Beta strandi276 – 28510Combined sources
Beta strandi292 – 2987Combined sources
Helixi320 – 3278Combined sources
Beta strandi344 – 35613Combined sources
Beta strandi359 – 3646Combined sources
Beta strandi367 – 3693Combined sources
Helixi376 – 3816Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi426 – 4338Combined sources
Beta strandi445 – 4495Combined sources
Beta strandi454 – 46310Combined sources
Helixi466 – 4716Combined sources
Beta strandi479 – 4857Combined sources
Beta strandi489 – 4968Combined sources
Beta strandi501 – 5099Combined sources
Helixi510 – 5145Combined sources
Beta strandi518 – 5236Combined sources
Helixi525 – 5273Combined sources
Helixi533 – 5364Combined sources
Helixi539 – 5457Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOZX-ray1.90A/B1-552[»]
1ASOX-ray2.20A/B1-552[»]
1ASPX-ray2.59A/B1-552[»]
1ASQX-ray2.32A/B1-552[»]
ProteinModelPortaliP37064.
SMRiP37064. Positions 1-552.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37064.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 122122Plastocyanin-like 1Add
BLAST
Domaini134 – 300167Plastocyanin-like 2Add
BLAST
Domaini344 – 523180Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR017760. L-ascorbate_oxidase_pln.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
TIGRFAMsiTIGR03388. ascorbase. 1 hit.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37064-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SQIRHYKWEV EYMFWAPNCN ENIVMGINGQ FPGPTIRANA GDSVVVELTN
60 70 80 90 100
KLHTEGVVIH WHGILQRGTP WADGTASISQ CAINPGETFF YNFTVDNPGT
110 120 130 140 150
FFYHGHLGMQ RSAGLYGSLI VDPPQGKKEP FHYDGEINLL LSDWWHQSIH
160 170 180 190 200
KQEVGLSSKP IRWIGEPQTI LLNGRGQFDC SIAAKYDSNL EPCKLKGSES
210 220 230 240 250
CAPYIFHVSP KKTYRIRIAS TTALAALNFA IGNHQLLVVE ADGNYVQPFY
260 270 280 290 300
TSDIDIYSGE SYSVLITTDQ NPSENYWVSV GTRARHPNTP PGLTLLNYLP
310 320 330 340 350
NSVSKLPTSP PPQTPAWDDF DRSKNFTYRI TAAMGSPKPP VKFNRRIFLL
360 370 380 390 400
NTQNVINGYV KWAINDVSLA LPPTPYLGAM KYNLLHAFDQ NPPPEVFPED
410 420 430 440 450
YDIDTPPTNE KTRIGNGVYQ FKIGEVVDVI LQNANMMKEN LSETHPWHLH
460 470 480 490 500
GHDFWVLGYG DGKFSAEEES SLNLKNPPLR NTVVIFPYGW TAIRFVADNP
510 520 530 540 550
GVWAFHCHIE PHLHMGMGVV FAEGVEKVGR IPTKALACGG TAKSLINNPK

NP
Length:552
Mass (Da):61,704
Last modified:June 1, 1994 - v1
Checksum:i24660B0F47AB54B4
GO

Sequence databases

PIRiA51027.

Cross-referencesi

Sequence databases

PIRiA51027.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOZX-ray1.90A/B1-552[»]
1ASOX-ray2.20A/B1-552[»]
1ASPX-ray2.59A/B1-552[»]
1ASQX-ray2.32A/B1-552[»]
ProteinModelPortaliP37064.
SMRiP37064. Positions 1-552.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

UniCarbKBiP37064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17019.
BRENDAi1.10.3.3. 1740.

Miscellaneous databases

EvolutionaryTraceiP37064.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR017760. L-ascorbate_oxidase_pln.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
TIGRFAMsiTIGR03388. ascorbase. 1 hit.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiASO_CUCPM
AccessioniPrimary (citable) accession number: P37064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 16, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.