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Q9FRX6 (AS1_ANTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aureusidin synthase

Short name=AmAS1
EC=1.21.3.6
Gene names
Name:AS1
OrganismAntirrhinum majus (Garden snapdragon)
Taxonomic identifier4151 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesPlantaginaceaeAntirrhineaeAntirrhinum

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of aurones, plant flavonoids that provide yellow coloration to flowers. Can use tetrahydroxychalcone (THC), pentahydroxychalcone (PHC), THC 4'-glucoside and PHC 4'-glucoside as substrates, but not 2'-hydroxychalcone, 4-hydroxychalcone, PHC 3-glucoside, 2',6'-dihydroxy-4,4'-dimethoxychalcone, naringenin, eriodictyol and 4,4',6-trihydroxyaurone. Can also produce bracteatin from PHC. Ref.1 Ref.6

Catalytic activity

2',4,4',6'-tetrahydroxychalcone 4'-O-beta-glucoside + O2 = aureusidin 6-O-beta-glucoside + H2O. Ref.1 Ref.3

2 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O2 = 2 aureusidin 6-O-beta-glucoside + 2 H2O. Ref.1 Ref.3

2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O2 = bracteatin 6-O-beta-glucoside + H2O. Ref.1 Ref.3

Cofactor

Binds 2 copper ions per subunit. Ref.1

Enzyme regulation

H2O2 activates the 3-hydroxylation and oxidative cyclization of tetrahydroxychalcone but inhibits reaction with pentahydroxychalcone. Inhibited by phenylthiourea. Ref.1 Ref.3

Subunit structure

Monomer. Ref.1

Subcellular location

Vacuole lumen Ref.4 Ref.6.

Tissue specificity

Expressed in petals. Not detected in stems and leaves. Ref.1

Domain

The N-terminal sequence (1-53) is sufficient for vacuolar targeting.

Post-translational modification

Glycosylated. Ref.1

Contains probably N- and C-terminal propeptides.

Sequence similarities

Belongs to the tyrosinase family.

Biophysicochemical properties

Kinetic parameters:

KM=4.3 µM for 2',4,4',6'-tetrahydroxychalcone Ref.1 Ref.3

KM=3.9 µM for 2',4,4',6'-tetrahydroxychalcone 4'-glucoside

KM=2.5 µM for isoliquiritigenin

KM=15.7 µM for 2',3,4,4',6'-pentahydroxychalcone

KM=8.1 µM for 2',3,4,4',6'-pentahydroxychalcone 4'-glucoside

KM=14.7 µM for butein

pH dependence:

Optimum pH is 5.4 for the reaction with tetrahydroxychalcone and 5.0 - 7.0 for the reaction with pentahydroxychalcone.

Ontologies

Keywords
   Cellular componentVacuole
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
Thioether bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpigment biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentvacuolar lumen

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionaureusidin synthase activity

Inferred from direct assay Ref.1. Source: UniProtKB

catechol oxidase activity

Inferred from electronic annotation. Source: InterPro

copper ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Aureusidin synthase
PRO_0000418416

Sites

Metal binding1471Copper A By similarity
Metal binding1681Copper A By similarity
Metal binding1771Copper A By similarity
Metal binding3011Copper B By similarity
Metal binding3051Copper B By similarity
Metal binding3351Copper B By similarity

Amino acid modifications

Disulfide bond71 ↔ 86 By similarity
Disulfide bond85 ↔ 148 By similarity
Cross-link151 ↔ 1682'-(S-cysteinyl)-histidine (Cys-His) By similarity

Experimental info

Mutagenesis501L → F: Loss of vacuolar targeting. Ref.4
Mutagenesis521Y → P: Loss of vacuolar targeting. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9FRX6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 660C2D72C3C054E3

FASTA56264,044
        10         20         30         40         50         60 
MFKNPNIRYH KLSSKSNDND QESSHRCKHI LLFIITLFLL IVGLYIANSL AYARFASTST 

        70         80         90        100        110        120 
GPIAAPDVTK CGQPDLPPGT APINCCPPIP AKIIDFELPP PSTTMRVRRA AHLVDDAYIA 

       130        140        150        160        170        180 
KFKKAVELMR ALPEDDPRSF KQQANVHCAY CAGAYNQAGF TNLKLQIHRS WLFFPFHRYY 

       190        200        210        220        230        240 
IYFFERILGK LINDTTFALP FWNYDSPGGM TIPSMFIDTN SSLYDSLRDS NHQPPTIVDL 

       250        260        270        280        290        300 
NYAFSDSDNT TTPEEQMIIN LKIVYRQMVS SAKTPQLFFG RPYRRGDQEF PGVGSIELVP 

       310        320        330        340        350        360 
HGMIHLWTGS ENTPYGENMG AFYSTARDPI FFAHHSNVDR MWSIWKTLGG PRRTDLTDPD 

       370        380        390        400        410        420 
FLDASFVFYD ENAEMVRVKV RDCLDEKKLG YVYQDVEIPW LNTRPTPKVS PSLLKKFHRT 

       430        440        450        460        470        480 
NTANPRQVFP AILDRVLKVI VTRPKKTRSR KEKDELEEIL VIEGIELERD HGHVKFDVYI 

       490        500        510        520        530        540 
NADEDDLAVI SPENAEFAGS FVSLWHKPIK GKRTKTQLLT LSICDILEDL DADEDDYVLV 

       550        560 
TLVPRNAGDA IKIHNVKIEL DG 

« Hide

References

[1]"Aureusidin synthase: a polyphenol oxidase homolog responsible for flower coloration."
Nakayama T., Yonekura-Sakakibara K., Sato T., Kikuchi S., Fukui Y., Fukuchi-Mizutani M., Ueda T., Nakao M., Tanaka Y., Kusumi T., Nishino T.
Science 290:1163-1166(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-121; 263-293 AND 389-400, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, TISSUE SPECIFICITY.
[2]"Genes involved in aurone biosynthesis."
Wang C.-K., To K.-Y.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Specificity analysis and mechanism of aurone synthesis catalyzed by aureusidin synthase, a polyphenol oxidase homolog responsible for flower coloration."
Nakayama T., Sato T., Fukui Y., Yonekura-Sakakibara K., Hayashi H., Tanaka Y., Kusumi T., Nishino T.
FEBS Lett. 499:107-111(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
[4]"Localization of a flavonoid biosynthetic polyphenol oxidase in vacuoles."
Ono E., Hatayama M., Isono Y., Sato T., Watanabe R., Yonekura-Sakakibara K., Fukuchi-Mizutani M., Tanaka Y., Kusumi T., Nishino T., Nakayama T.
Plant J. 45:133-143(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-50 AND TYR-52.
[5]"Homology modeling and dynamics study of aureusidin synthase--an important enzyme in aurone biosynthesis of snapdragon flower."
Elumalai P., Liu H.L.
Int. J. Biol. Macromol. 49:134-142(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[6]"Yellow flowers generated by expression of the aurone biosynthetic pathway."
Ono E., Fukuchi-Mizutani M., Nakamura N., Fukui Y., Yonekura-Sakakibara K., Yamaguchi M., Nakayama T., Tanaka T., Kusumi T., Tanaka Y.
Proc. Natl. Acad. Sci. U.S.A. 103:11075-11080(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB044884 mRNA. Translation: BAB20048.1.
EF650014 mRNA. Translation: ABR57233.1.

3D structure databases

ProteinModelPortalQ9FRX6.
SMRQ9FRX6. Positions 61-401.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAS1_ANTMA
AccessionPrimary (citable) accession number: Q9FRX6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families