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Q9FRX6

- AS1_ANTMA

UniProt

Q9FRX6 - AS1_ANTMA

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Protein

Aureusidin synthase

Gene
AS1
Organism
Antirrhinum majus (Garden snapdragon)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

2',4,4',6'-tetrahydroxychalcone 4'-O-beta-glucoside + O2 = aureusidin 6-O-beta-glucoside + H2O.2 Publications
2 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O2 = 2 aureusidin 6-O-beta-glucoside + 2 H2O.2 Publications
2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O2 = bracteatin 6-O-beta-glucoside + H2O.2 Publications

Cofactori

Binds 2 copper ions per subunit.1 Publication

Enzyme regulationi

H2O2 activates the 3-hydroxylation and oxidative cyclization of tetrahydroxychalcone but inhibits reaction with pentahydroxychalcone. Inhibited by phenylthiourea.2 Publications

Kineticsi

  1. KM=4.3 µM for 2',4,4',6'-tetrahydroxychalcone2 Publications
  2. KM=3.9 µM for 2',4,4',6'-tetrahydroxychalcone 4'-glucoside
  3. KM=2.5 µM for isoliquiritigenin
  4. KM=15.7 µM for 2',3,4,4',6'-pentahydroxychalcone
  5. KM=8.1 µM for 2',3,4,4',6'-pentahydroxychalcone 4'-glucoside
  6. KM=14.7 µM for butein

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi147 – 1471Copper A By similarity
Metal bindingi168 – 1681Copper A By similarity
Metal bindingi177 – 1771Copper A By similarity
Metal bindingi301 – 3011Copper B By similarity
Metal bindingi305 – 3051Copper B By similarity
Metal bindingi335 – 3351Copper B By similarity

GO - Molecular functioni

  1. aureusidin synthase activity Source: UniProtKB
  2. catechol oxidase activity Source: InterPro
  3. copper ion binding Source: UniProtKB

GO - Biological processi

  1. pigment biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aureusidin synthase (EC:1.21.3.6)
Short name:
AmAS1
Gene namesi
Name:AS1
OrganismiAntirrhinum majus (Garden snapdragon)
Taxonomic identifieri4151 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesPlantaginaceaeAntirrhineaeAntirrhinum

Subcellular locationi

Vacuole lumen 2 Publications

GO - Cellular componenti

  1. vacuolar lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501L → F: Loss of vacuolar targeting. 1 Publication
Mutagenesisi52 – 521Y → P: Loss of vacuolar targeting. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Aureusidin synthasePRO_0000418416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 86 By similarity
Disulfide bondi85 ↔ 148 By similarity
Cross-linki151 ↔ 1682'-(S-cysteinyl)-histidine (Cys-His) By similarity

Post-translational modificationi

Glycosylated.1 Publication
Contains probably N- and C-terminal propeptides.

Keywords - PTMi

Disulfide bond, Glycoprotein, Thioether bond

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9FRX6.
SMRiQ9FRX6. Positions 61-401.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the tyrosinase family.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000290. PPO_plant. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FRX6-1 [UniParc]FASTAAdd to Basket

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MFKNPNIRYH KLSSKSNDND QESSHRCKHI LLFIITLFLL IVGLYIANSL    50
AYARFASTST GPIAAPDVTK CGQPDLPPGT APINCCPPIP AKIIDFELPP 100
PSTTMRVRRA AHLVDDAYIA KFKKAVELMR ALPEDDPRSF KQQANVHCAY 150
CAGAYNQAGF TNLKLQIHRS WLFFPFHRYY IYFFERILGK LINDTTFALP 200
FWNYDSPGGM TIPSMFIDTN SSLYDSLRDS NHQPPTIVDL NYAFSDSDNT 250
TTPEEQMIIN LKIVYRQMVS SAKTPQLFFG RPYRRGDQEF PGVGSIELVP 300
HGMIHLWTGS ENTPYGENMG AFYSTARDPI FFAHHSNVDR MWSIWKTLGG 350
PRRTDLTDPD FLDASFVFYD ENAEMVRVKV RDCLDEKKLG YVYQDVEIPW 400
LNTRPTPKVS PSLLKKFHRT NTANPRQVFP AILDRVLKVI VTRPKKTRSR 450
KEKDELEEIL VIEGIELERD HGHVKFDVYI NADEDDLAVI SPENAEFAGS 500
FVSLWHKPIK GKRTKTQLLT LSICDILEDL DADEDDYVLV TLVPRNAGDA 550
IKIHNVKIEL DG 562
Length:562
Mass (Da):64,044
Last modified:March 1, 2001 - v1
Checksum:i660C2D72C3C054E3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB044884 mRNA. Translation: BAB20048.1.
EF650014 mRNA. Translation: ABR57233.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB044884 mRNA. Translation: BAB20048.1 .
EF650014 mRNA. Translation: ABR57233.1 .

3D structure databases

ProteinModelPortali Q9FRX6.
SMRi Q9FRX6. Positions 61-401.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000290. PPO_plant. 1 hit.
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 1 hit.
PROSITEi PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAS1_ANTMA
AccessioniPrimary (citable) accession number: Q9FRX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 58 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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