3MAT_DAHPI
ID 3MAT_DAHPI Reviewed; 460 AA.
AC Q8GSN8;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Malonyl-coenzyme A:anthocyanin 3-O-glucoside-6''-O-malonyltransferase {ECO:0000303|PubMed:12481098};
DE Short=Dv3MaT {ECO:0000303|PubMed:12481098};
DE Short=Malonyl CoA:anthocyanin 3-O-glucoside-6''-O-malonyltransferase {ECO:0000312|EMBL:AAO12206.1};
DE EC=2.3.1.171;
GN Name=3MAT {ECO:0000303|PubMed:12481098};
OS Dahlia pinnata (Pinnate dahlia) (Dahlia variabilis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Coreopsideae; Dahlia.
OX NCBI_TaxID=101596;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO12206.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Kaen {ECO:0000269|PubMed:12481098};
RC TISSUE=Petal {ECO:0000269|PubMed:12481098};
RX PubMed=12481098; DOI=10.1104/pp.010447;
RA Suzuki H., Nakayama T., Yonekura-Sakakibara K., Fukui Y., Nakamura N.,
RA Yamaguchi M.A., Tanaka Y., Kusumi T., Nishino T.;
RT "cDNA cloning, heterologous expressions, and functional characterization of
RT malonyl-coenzyme a:anthocyanidin 3-o-glucoside-6''-o-malonyltransferase
RT from dahlia flowers.";
RL Plant Physiol. 130:2142-2151(2002).
CC -!- FUNCTION: Catalyzes the transfer of the malonyl group from malonyl-CoA
CC to pelargonidin 3-O-glucoside to produce pelargonidin 3-O-6''-O-
CC malonylglucoside. Can also transfer the malonyl group from malonyl-CoA
CC to cyanidin 3-O-glucoside, delphinidin 3-O-glucoside and quercetin 3-O-
CC glucoside. {ECO:0000269|PubMed:12481098}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an anthocyanidin 3-O-beta-D-glucoside + malonyl-CoA = an
CC anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside) + CoA;
CC Xref=Rhea:RHEA:16025, ChEBI:CHEBI:16307, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:84163; EC=2.3.1.171;
CC Evidence={ECO:0000269|PubMed:12481098};
CC -!- ACTIVITY REGULATION: Completely inhibited by 5 mM N-ethylmaleimide or
CC 0.1 mM Cu(2+). Partially inhibited by 0.1 mM Fe(2+) or 0.1 mM Hg(2+).
CC {ECO:0000269|PubMed:12481098}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.8 uM for malonyl-CoA {ECO:0000269|PubMed:12481098};
CC KM=46.7 uM for pelargonidin {ECO:0000269|PubMed:12481098};
CC pH dependence:
CC Optimum pH is 8.5. Active over the pH range 5.5-11.0. Stable from pH
CC 6.5 to 7.5 for 20 hours at 20 degrees Celsius.
CC {ECO:0000269|PubMed:12481098};
CC Temperature dependence:
CC Stable below 45 degrees Celsius for 20 minutes at pH 7.0.
CC {ECO:0000269|PubMed:12481098};
CC -!- DEVELOPMENTAL STAGE: Expression is highest in petals at stage 2 of
CC flower development (when the top of the bud is open, flowers are 6-9 mm
CC in length and almost pigmented). {ECO:0000269|PubMed:12481098}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000255}.
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DR EMBL; AF489108; AAO12206.1; -; mRNA.
DR AlphaFoldDB; Q8GSN8; -.
DR SMR; Q8GSN8; -.
DR KEGG; ag:AAO12206; -.
DR BioCyc; MetaCyc:MON-12015; -.
DR BRENDA; 2.3.1.171; 1828.
DR GO; GO:0033809; F:anthocyanin 6''-O-malonyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102588; F:cyanidin 3-O-glucoside 6''-O-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Phenylpropanoid metabolism; Transferase.
FT CHAIN 1..460
FT /note="Malonyl-coenzyme A:anthocyanin 3-O-glucoside-6''-O-
FT malonyltransferase"
FT /id="PRO_0000405126"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 51302 MW; 421F2B012B3B020E CRC64;
MDNIPNLTIL EHSRISPPPS TIGHRSLPLT FFDIAWLLFP PVHHLYFYHF PYSKSHFTET
VIPNLKHSLS ITLQHYFPFV GKLIVYPNPH DSTRKPEIRH VEGDSVALTF AETTLDFNDL
SANHPRKCEN FYPLVPPLGN AVKESDYVTL PVFSVQVTYF PNSGISIGLT NHHSLSDANT
RFGFLKAWAS VCETGEDQPF LKNGSPPVFD RVVVNPQLYE NRLNQTRLGT FYQAPSLVGS
SSDRVRATFV LARTHISGLK KQVLTQLPML EYTSSFTVTC GYIWSCIVKS LVNMGEKKGE
DELEQFIVSV GCRSRLDPPL PENYFGNCSA PCIVTIKNGV LKGENGFVMA AKLIGEGISK
MVNKKGGILE YADRWYDGFK IPARKMGISG TPKLNFYDID FGWGKAMKYE VVSIDYSASV
SLSACKESAQ DFEIGVCFPS MQMEAFGKIF NDGLESAIAS