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Protein

Aureusidin synthase

Gene

AS1

Organism
Antirrhinum majus (Garden snapdragon)
Status
Reviewed-Annotation score: 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 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O2 = 2 aureusidin 6-O-beta-glucoside + 2 H2O.
2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O2 = bracteatin 6-O-beta-glucoside + H2O.

Cofactori

Cu2+1 PublicationNote: 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'-glucoside2 Publications
  3. KM=2.5 µM for isoliquiritigenin2 Publications
  4. KM=15.7 µM for 2',3,4,4',6'-pentahydroxychalcone2 Publications
  5. KM=8.1 µM for 2',3,4,4',6'-pentahydroxychalcone 4'-glucoside2 Publications
  6. KM=14.7 µM for butein2 Publications

    pH dependencei

    Optimum pH is 5.4 for the reaction with tetrahydroxychalcone and 5.0 - 7.0 for the reaction with pentahydroxychalcone.2 Publications

    Sites

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

    GO - Molecular functioni

    • aureusidin synthase activity Source: UniProtKB
    • catechol oxidase activity Source: InterPro
    • copper ion binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.21.3.6. 376.

    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

    GO - Cellular componenti

    • 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 ↔ 86By similarity
    Disulfide bondi85 ↔ 148By 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    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

    « Hide

            10         20         30         40         50
    MFKNPNIRYH KLSSKSNDND QESSHRCKHI LLFIITLFLL IVGLYIANSL
    60 70 80 90 100
    AYARFASTST GPIAAPDVTK CGQPDLPPGT APINCCPPIP AKIIDFELPP
    110 120 130 140 150
    PSTTMRVRRA AHLVDDAYIA KFKKAVELMR ALPEDDPRSF KQQANVHCAY
    160 170 180 190 200
    CAGAYNQAGF TNLKLQIHRS WLFFPFHRYY IYFFERILGK LINDTTFALP
    210 220 230 240 250
    FWNYDSPGGM TIPSMFIDTN SSLYDSLRDS NHQPPTIVDL NYAFSDSDNT
    260 270 280 290 300
    TTPEEQMIIN LKIVYRQMVS SAKTPQLFFG RPYRRGDQEF PGVGSIELVP
    310 320 330 340 350
    HGMIHLWTGS ENTPYGENMG AFYSTARDPI FFAHHSNVDR MWSIWKTLGG
    360 370 380 390 400
    PRRTDLTDPD FLDASFVFYD ENAEMVRVKV RDCLDEKKLG YVYQDVEIPW
    410 420 430 440 450
    LNTRPTPKVS PSLLKKFHRT NTANPRQVFP AILDRVLKVI VTRPKKTRSR
    460 470 480 490 500
    KEKDELEEIL VIEGIELERD HGHVKFDVYI NADEDDLAVI SPENAEFAGS
    510 520 530 540 550
    FVSLWHKPIK GKRTKTQLLT LSICDILEDL DADEDDYVLV TLVPRNAGDA
    560
    IKIHNVKIEL DG
    Length:562
    Mass (Da):64,044
    Last modified:March 1, 2001 - v1
    Checksum:i660C2D72C3C054E3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB044884 mRNA. Translation: BAB20048.1.
    EF650014 mRNA. Translation: ABR57233.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB044884 mRNA. Translation: BAB20048.1.
    EF650014 mRNA. Translation: ABR57233.1.

    3D structure databases

    ProteinModelPortaliQ9FRX6.
    SMRiQ9FRX6. Positions 61-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi1.21.3.6. 376.

    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]
    ProtoNetiSearch...

    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: April 1, 2015
    This is version 61 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

    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 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.