ID A4PHY4_CHRMO Unreviewed; 454 AA.
AC A4PHY4;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Anthocyanin malonyltransferase homolog {ECO:0000313|EMBL:BAF50706.1};
GN Name=Dm3MaT3 {ECO:0000313|EMBL:BAF50706.1};
OS Chrysanthemum morifolium (Florist's daisy) (Dendranthema grandiflorum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Chrysanthemum.
OX NCBI_TaxID=41568 {ECO:0000313|EMBL:BAF50706.1};
RN [1] {ECO:0000313|EMBL:BAF50706.1, ECO:0007829|PDB:2E1T}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17383962; DOI=10.1074/jbc.M700638200;
RA Unno H., Ichimaida F., Suzuki H., Takahashi S., Tanaka Y., Saito A.,
RA Nishino T., Kusunoki M., Nakayama T.;
RT "Structural and mutational studies of anthocyanin malonyltransferases
RT establish the features of BAHD enzyme catalysis.";
RL J. Biol. Chem. 282:15812-15822(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB290338; BAF50706.1; -; mRNA.
DR PDB; 2E1T; X-ray; 2.10 A; A/B=1-454.
DR PDB; 2E1U; X-ray; 2.20 A; A/B=1-454.
DR PDB; 2E1V; X-ray; 1.80 A; A/B=1-454.
DR PDBsum; 2E1T; -.
DR PDBsum; 2E1U; -.
DR PDBsum; 2E1V; -.
DR AlphaFoldDB; A4PHY4; -.
DR SMR; A4PHY4; -.
DR EvolutionaryTrace; A4PHY4; -.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR PANTHER; PTHR31625; -; 1.
DR PANTHER; PTHR31625:SF90; ACYLTRANSFERASE-LIKE PROTEIN-RELATED; 1.
DR Pfam; PF02458; Transferase; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2E1T, ECO:0007829|PDB:2E1U};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAF50706.1}.
FT BINDING 170
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 175
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 178
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 260
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 271
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 272
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 273
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 274
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 275
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 303
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 307
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 386
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT BINDING 389
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0007829|PDB:2E1T"
FT DISULFID 125..433
FT /evidence="ECO:0007829|PDB:2E1T, ECO:0007829|PDB:2E1U"
SQ SEQUENCE 454 AA; 50806 MW; 0445B40D43F0F069 CRC64;
MASLPILTVL EQSQVSPPPD TLGDKSLQLT FFDFFWLRSP PINNLFFYEL PITRSQFTET
VVPNIKHSLS ITLKHFYPFV GKLVVYPAPT KKPEICYVEG DSVAVTFAEC NLDLNELTGN
HPRNCDKFYD LVPILGESTR LSDCIKIPLF SVQVTLFPNQ GIAIGITNHH CLGDASTRFC
FLKAWTSIAR SGNNDESFLA NGTRPLYDRI IKYPMLDEAY LKRAKVESFN EDYVTQSLAG
PSDKLRATFI LTRAVINQLK DRVLAQLPTL EYVSSFTVAC AYIWSCIAKS RNDKLQLFGF
PIDRRARMKP PIPTAYFGNC VGGCAAIAKT NLLIGKEGFI TAAKLIGENL HKTLTDYKDG
VLKDDMESFN DLVSEGMPTT MTWVSGTPKL RFYDMDFGWG KPKKLETVSI DHNGAISINS
CKESNEDLEI GVCISATQME DFVHIFDDGL KAYL
//
