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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)DescriptionActionsGraphical viewLength
Metal bindingi60Copper 1; type 21 Publication1
Metal bindingi62Copper 2; type 31 Publication1
Metal bindingi104Copper 2; type 31 Publication1
Metal bindingi106Copper 3; type 31 Publication1
Metal bindingi445Copper 4; type 11 Publication1
Metal bindingi448Copper 1; type 21 Publication1
Metal bindingi450Copper 3; type 31 Publication1
Metal bindingi506Copper 3; type 31 Publication1
Metal bindingi507Copper 4; type 11 Publication1
Metal bindingi508Copper 2; type 31 Publication1
Metal bindingi512Copper 4; type 11 Publication1
Metal bindingi517Copper 4; type 11 Publication1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000855821 – 552L-ascorbate oxidaseAdd BLAST552

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi19 ↔ 2011 Publication
Disulfide bondi81 ↔ 5381 Publication
GlycosylationiCAR_00014992N-linked (GlcNAc...)1 Publication1
Disulfide bondi180 ↔ 1931 Publication
Glycosylationi325N-linked (GlcNAc...)Sequence analysis1
Glycosylationi440N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP37064.

Interactioni

Subunit structurei

Dimer.1 Publication

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 15Combined sources13
Beta strandi22 – 27Combined sources6
Beta strandi30 – 32Combined sources3
Beta strandi36 – 39Combined sources4
Beta strandi43 – 50Combined sources8
Beta strandi59 – 62Combined sources4
Helixi70 – 72Combined sources3
Turni76 – 78Combined sources3
Beta strandi88 – 94Combined sources7
Beta strandi99 – 105Combined sources7
Turni108 – 110Combined sources3
Helixi111 – 113Combined sources3
Beta strandi116 – 122Combined sources7
Beta strandi134 – 144Combined sources11
Helixi149 – 155Combined sources7
Beta strandi158 – 160Combined sources3
Beta strandi168 – 172Combined sources5
Beta strandi178 – 181Combined sources4
Helixi184 – 186Combined sources3
Beta strandi206 – 208Combined sources3
Beta strandi213 – 220Combined sources8
Beta strandi226 – 231Combined sources6
Beta strandi236 – 241Combined sources6
Beta strandi244 – 252Combined sources9
Beta strandi254 – 256Combined sources3
Beta strandi261 – 267Combined sources7
Beta strandi276 – 285Combined sources10
Beta strandi292 – 298Combined sources7
Helixi320 – 327Combined sources8
Beta strandi344 – 356Combined sources13
Beta strandi359 – 364Combined sources6
Beta strandi367 – 369Combined sources3
Helixi376 – 381Combined sources6
Beta strandi413 – 415Combined sources3
Beta strandi419 – 421Combined sources3
Beta strandi426 – 433Combined sources8
Beta strandi445 – 449Combined sources5
Beta strandi454 – 463Combined sources10
Helixi466 – 471Combined sources6
Beta strandi479 – 485Combined sources7
Beta strandi489 – 496Combined sources8
Beta strandi501 – 509Combined sources9
Helixi510 – 514Combined sources5
Beta strandi518 – 523Combined sources6
Helixi525 – 527Combined sources3
Helixi533 – 536Combined sources4
Helixi539 – 545Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37064.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 122Plastocyanin-like 1Add BLAST122
Domaini134 – 300Plastocyanin-like 2Add BLAST167
Domaini344 – 523Plastocyanin-like 3Add BLAST180

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
PDB 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.
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: November 2, 2016
This is version 94 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.