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Q9FRX6

- AS1_ANTMA

UniProt

Q9FRX6 - AS1_ANTMA

Protein

Aureusidin synthase

Gene

AS1

Organism
Antirrhinum majus (Garden snapdragon)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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

    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

    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

    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

    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

    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: October 1, 2014
    This is version 59 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