AS1_ANTMA
ID AS1_ANTMA Reviewed; 562 AA.
AC Q9FRX6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Aureusidin synthase;
DE Short=AmAS1;
DE EC=1.21.3.6 {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
GN Name=AS1;
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-121; 263-293 AND
RP 389-400, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11073455; DOI=10.1126/science.290.5494.1163;
RA Nakayama T., Yonekura-Sakakibara K., Sato T., Kikuchi S., Fukui Y.,
RA Fukuchi-Mizutani M., Ueda T., Nakao M., Tanaka Y., Kusumi T., Nishino T.;
RT "Aureusidin synthase: a polyphenol oxidase homolog responsible for flower
RT coloration.";
RL Science 290:1163-1166(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang C.-K., To K.-Y.;
RT "Genes involved in aurone biosynthesis.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND ACTIVITY REGULATION.
RX PubMed=11418122; DOI=10.1016/s0014-5793(01)02529-7;
RA Nakayama T., Sato T., Fukui Y., Yonekura-Sakakibara K., Hayashi H.,
RA Tanaka Y., Kusumi T., Nishino T.;
RT "Specificity analysis and mechanism of aurone synthesis catalyzed by
RT aureusidin synthase, a polyphenol oxidase homolog responsible for flower
RT coloration.";
RL FEBS Lett. 499:107-111(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-50 AND TYR-52.
RX PubMed=16367960; DOI=10.1111/j.1365-313x.2005.02625.x;
RA Ono E., Hatayama M., Isono Y., Sato T., Watanabe R.,
RA Yonekura-Sakakibara K., Fukuchi-Mizutani M., Tanaka Y., Kusumi T.,
RA Nishino T., Nakayama T.;
RT "Localization of a flavonoid biosynthetic polyphenol oxidase in vacuoles.";
RL Plant J. 45:133-143(2006).
RN [5]
RP 3D-STRUCTURE MODELING.
RX PubMed=21470561; DOI=10.1016/j.ijbiomac.2011.03.017;
RA Elumalai P., Liu H.L.;
RT "Homology modeling and dynamics study of aureusidin synthase--an important
RT enzyme in aurone biosynthesis of snapdragon flower.";
RL Int. J. Biol. Macromol. 49:134-142(2011).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16832053; DOI=10.1073/pnas.0604246103;
RA Ono E., Fukuchi-Mizutani M., Nakamura N., Fukui Y., Yonekura-Sakakibara K.,
RA Yamaguchi M., Nakayama T., Tanaka T., Kusumi T., Tanaka Y.;
RT "Yellow flowers generated by expression of the aurone biosynthetic
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11075-11080(2006).
CC -!- FUNCTION: Involved in the biosynthesis of aurones, plant flavonoids
CC that provide yellow coloration to flowers. Can use tetrahydroxychalcone
CC (THC), pentahydroxychalcone (PHC), THC 4'-glucoside and PHC 4'-
CC glucoside as substrates, but not 2'-hydroxychalcone, 4-hydroxychalcone,
CC PHC 3-glucoside, 2',6'-dihydroxy-4,4'-dimethoxychalcone, naringenin,
CC eriodictyol and 4,4',6-trihydroxyaurone. Can also produce bracteatin
CC from PHC. {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:16832053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',4,4',6'-tetrahydroxychalcone 4'-O-beta-D-glucoside + H(+) +
CC O2 = aureusidin 6-O-beta-glucoside + H2O; Xref=Rhea:RHEA:34203,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:66905, ChEBI:CHEBI:77978; EC=1.21.3.6;
CC Evidence={ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + 2
CC H(+) + O2 = 2 aureusidin 6-O-beta-glucoside + 2 H2O;
CC Xref=Rhea:RHEA:34195, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:66905, ChEBI:CHEBI:77622; EC=1.21.3.6;
CC Evidence={ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + H(+)
CC + O2 = bracteatin 6-O-beta-glucoside + H2O; Xref=Rhea:RHEA:34199,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:66907, ChEBI:CHEBI:77622; EC=1.21.3.6;
CC Evidence={ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:11073455};
CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:11073455};
CC -!- ACTIVITY REGULATION: H(2)O(2) activates the 3-hydroxylation and
CC oxidative cyclization of tetrahydroxychalcone but inhibits reaction
CC with pentahydroxychalcone. Inhibited by phenylthiourea.
CC {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 uM for 2',4,4',6'-tetrahydroxychalcone
CC {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC KM=3.9 uM for 2',4,4',6'-tetrahydroxychalcone 4'-glucoside
CC {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC KM=2.5 uM for isoliquiritigenin {ECO:0000269|PubMed:11073455,
CC ECO:0000269|PubMed:11418122};
CC KM=15.7 uM for 2',3,4,4',6'-pentahydroxychalcone
CC {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC KM=8.1 uM for 2',3,4,4',6'-pentahydroxychalcone 4'-glucoside
CC {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC KM=14.7 uM for butein {ECO:0000269|PubMed:11073455,
CC ECO:0000269|PubMed:11418122};
CC pH dependence:
CC Optimum pH is 5.4 for the reaction with tetrahydroxychalcone and 5.0
CC - 7.0 for the reaction with pentahydroxychalcone.
CC {ECO:0000269|PubMed:11073455, ECO:0000269|PubMed:11418122};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11073455}.
CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:16367960,
CC ECO:0000269|PubMed:16832053}.
CC -!- TISSUE SPECIFICITY: Expressed in petals. Not detected in stems and
CC leaves. {ECO:0000269|PubMed:11073455}.
CC -!- DOMAIN: The N-terminal sequence (1-53) is sufficient for vacuolar
CC targeting.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11073455}.
CC -!- PTM: Contains probably N- and C-terminal propeptides.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; AB044884; BAB20048.1; -; mRNA.
DR EMBL; EF650014; ABR57233.1; -; mRNA.
DR AlphaFoldDB; Q9FRX6; -.
DR SMR; Q9FRX6; -.
DR KEGG; ag:BAB20048; -.
DR BRENDA; 1.14.18.1; 376.
DR BRENDA; 1.21.3.6; 376.
DR GO; GO:0005775; C:vacuolar lumen; IDA:UniProtKB.
DR GO; GO:0033793; F:aureusidin synthase activity; IDA:UniProtKB.
DR GO; GO:0102706; F:butein:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0102791; F:sulfuretin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046148; P:pigment biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF12142; PPO1_DWL; 1.
DR Pfam; PF12143; PPO1_KFDV; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000290; PPO_plant; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxidoreductase; Thioether bond; Vacuole.
FT CHAIN 1..562
FT /note="Aureusidin synthase"
FT /id="PRO_0000418416"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 168
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 177
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 301
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 305
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 335
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 71..86
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 85..148
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 151..168
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT MUTAGEN 50
FT /note="L->F: Loss of vacuolar targeting."
FT /evidence="ECO:0000269|PubMed:16367960"
FT MUTAGEN 52
FT /note="Y->P: Loss of vacuolar targeting."
FT /evidence="ECO:0000269|PubMed:16367960"
SQ SEQUENCE 562 AA; 64044 MW; 660C2D72C3C054E3 CRC64;
MFKNPNIRYH KLSSKSNDND QESSHRCKHI LLFIITLFLL IVGLYIANSL AYARFASTST
GPIAAPDVTK CGQPDLPPGT APINCCPPIP AKIIDFELPP PSTTMRVRRA AHLVDDAYIA
KFKKAVELMR ALPEDDPRSF KQQANVHCAY CAGAYNQAGF TNLKLQIHRS WLFFPFHRYY
IYFFERILGK LINDTTFALP FWNYDSPGGM TIPSMFIDTN SSLYDSLRDS NHQPPTIVDL
NYAFSDSDNT TTPEEQMIIN LKIVYRQMVS SAKTPQLFFG RPYRRGDQEF PGVGSIELVP
HGMIHLWTGS ENTPYGENMG AFYSTARDPI FFAHHSNVDR MWSIWKTLGG PRRTDLTDPD
FLDASFVFYD ENAEMVRVKV RDCLDEKKLG YVYQDVEIPW LNTRPTPKVS PSLLKKFHRT
NTANPRQVFP AILDRVLKVI VTRPKKTRSR KEKDELEEIL VIEGIELERD HGHVKFDVYI
NADEDDLAVI SPENAEFAGS FVSLWHKPIK GKRTKTQLLT LSICDILEDL DADEDDYVLV
TLVPRNAGDA IKIHNVKIEL DG
