MAT1_TOBAC
ID MAT1_TOBAC Reviewed; 453 AA.
AC Q589Y0;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Phenolic glucoside malonyltransferase 1 {ECO:0000305};
DE Short=NtMaT1 {ECO:0000303|PubMed:15860007, ECO:0000303|PubMed:22610270};
DE EC=2.3.1.- {ECO:0000269|PubMed:15860007};
DE EC=2.3.1.116 {ECO:0000269|PubMed:15860007};
DE AltName: Full=Flavonol/naphthol glucoside malonyltransferase 1 {ECO:0000303|PubMed:22610270};
DE AltName: Full=Phenolic glucoside-6'-O-malonyltransferase 1 {ECO:0000303|PubMed:15860007};
GN Name=mat1 {ECO:0000312|EMBL:BAD93691.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000312|EMBL:BAD93691.1};
RN [1] {ECO:0000312|EMBL:BAD93691.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Bright Yellow {ECO:0000303|PubMed:15860007};
RC TISSUE=Callus {ECO:0000303|PubMed:15860007};
RX PubMed=15860007; DOI=10.1111/j.1365-313x.2005.02387.x;
RA Taguchi G., Shitchi Y., Shirasawa S., Yamamoto H., Hayashida N.;
RT "Molecular cloning, characterization, and downregulation of an
RT acyltransferase that catalyzes the malonylation of flavonoid and naphthol
RT glucosides in tobacco cells.";
RL Plant J. 42:481-491(2005).
RN [2] {ECO:0000312|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000312|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [3] {ECO:0007744|PDB:2XR7}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH MALONYL-COA,
RP SUBUNIT, AND MOTIF.
RX PubMed=22610270; DOI=10.1007/s00425-012-1660-8;
RA Manjasetty B.A., Yu X.H., Panjikar S., Taguchi G., Chance M.R., Liu C.J.;
RT "Structural basis for modification of flavonol and naphthol glucoconjugates
RT by Nicotiana tabacum malonyltransferase (NtMaT1).";
RL Planta 236:781-793(2012).
CC -!- FUNCTION: Malonyltransferase with broad substrate specificity acting on
CC phenolic glucosides including xenobiotic naphthols. Has activity
CC against flavonoid 7-O-glucosides, flavonoid 3-O-glucosides and naphthol
CC glucosides, and to a lesser extent against coumarin glucosides in
CC vitro. Prefers malonyl-CoA as an acyl donor, but also active with
CC succinyl-CoA and methylmalonyl-CoA, but not with acetyl-CoA.
CC {ECO:0000269|PubMed:15860007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavonol 3-O-beta-D-glucoside + malonyl-CoA = a flavonol 3-
CC O-(6-O-malonyl-beta-D-glucoside) + CoA; Xref=Rhea:RHEA:20085,
CC ChEBI:CHEBI:16816, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:58034; EC=2.3.1.116;
CC Evidence={ECO:0000269|PubMed:15860007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20086;
CC Evidence={ECO:0000269|PubMed:15860007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavonol 7-O-beta-D-glucoside + malonyl-CoA = a flavonol 7-
CC O-(6-O-malonyl-beta-D-glucoside) + CoA; Xref=Rhea:RHEA:58796,
CC ChEBI:CHEBI:52144, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:142805; Evidence={ECO:0000269|PubMed:15860007};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58797;
CC Evidence={ECO:0000269|PubMed:15860007};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26.5 uM for kaempferol 7-O-glucoside (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15860007};
CC KM=80.6 uM for kaempferol 3-O-glucoside (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15860007};
CC KM=179 uM for 2-naphthol glucoside (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15860007};
CC KM=5.5 uM for malonyl-CoA (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15860007};
CC KM=26.7 uM for succinyl-CoA (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:15860007};
CC Vmax=216 nmol/sec/mg enzyme toward kaempferol 7-O-glucoside (at 30
CC degrees Celsius) {ECO:0000269|PubMed:15860007};
CC Vmax=134 nmol/sec/mg enzyme toward kaempferol 3-O-glucoside (at 30
CC degrees Celsius) {ECO:0000269|PubMed:15860007};
CC Vmax=128 nmol/sec/mg enzyme toward 2-naphthol glucoside (at 30
CC degrees Celsius) {ECO:0000269|PubMed:15860007};
CC Vmax=159 nmol/sec/mg enzyme toward malonyl-CoA (at 30 degrees
CC Celsius) {ECO:0000269|PubMed:15860007};
CC Vmax=183 nmol/sec/mg enzyme toward succinyl-CoA (at 30 degrees
CC Celsius) {ECO:0000269|PubMed:15860007};
CC Note=kcat is 11.0 sec(-1) for kaempferol 7-O-glucoside. kcat is 6.8
CC sec(-1) for kaempferol 3-O-glucoside. kcat is 6.5 sec(-1) for 2-
CC naphthol glucoside. kcat is 8.0 sec(-1) for malonyl-CoA. kcat is 9.3
CC sec(-1) for succinyl-CoA. {ECO:0000269|PubMed:15860007};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:15860007};
CC Temperature dependence:
CC Stable below 40 degrees Celsius and pH 8.0 for 30 min.
CC {ECO:0000269|PubMed:15860007};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22610270}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flower. Also expressed in
CC flower bud, stem, root and leaf. {ECO:0000269|PubMed:15860007}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 2-week old seedlings.
CC {ECO:0000269|PubMed:15860007}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000305|PubMed:22610270}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. Phenolic
CC glucoside malonyltransferase subfamily. {ECO:0000305}.
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; AB176525; BAD93691.1; -; mRNA.
DR RefSeq; NP_001312260.1; NM_001325331.1.
DR PDB; 2XR7; X-ray; 3.10 A; A=1-453.
DR PDBsum; 2XR7; -.
DR AlphaFoldDB; Q589Y0; -.
DR SMR; Q589Y0; -.
DR STRING; 4097.Q589Y0; -.
DR GeneID; 107782063; -.
DR KEGG; nta:107782063; -.
DR OMA; GSIMFIK; -.
DR OrthoDB; 1130893at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0047165; F:flavonol-3-O-beta-glucoside O-malonyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016420; F:malonyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Detoxification; Reference proteome;
KW Transferase.
FT CHAIN 1..453
FT /note="Phenolic glucoside malonyltransferase 1"
FT /id="PRO_0000446371"
FT MOTIF 165..169
FT /note="HXXXD motif"
FT /evidence="ECO:0000305|PubMed:22610270"
FT MOTIF 394..398
FT /note="DFGWG motif"
FT /evidence="ECO:0000305|PubMed:22610270"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT BINDING 254
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000269|PubMed:22610270,
FT ECO:0000312|PDB:2XR7"
FT BINDING 266
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000269|PubMed:22610270,
FT ECO:0000312|PDB:2XR7"
FT BINDING 268..269
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000269|PubMed:22610270,
FT ECO:0000312|PDB:2XR7"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:2XR7"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:2XR7"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:2XR7"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:2XR7"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2XR7"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:2XR7"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:2XR7"
FT HELIX 436..450
FT /evidence="ECO:0007829|PDB:2XR7"
SQ SEQUENCE 453 AA; 50763 MW; 8B65788A422F8C59 CRC64;
MASVIEQCQV VPSPGSATEL TLPLTYFDHV WLAFHRMRRI LFYKLPISRP DFVQTIIPTL
KDSLSLTLKY YLPLAGNVAC PQDWSGYPEL RYVTGNSVSV IFSESDMDFN YLIGYHPRNT
KDFYHFVPQL AEPKDAPGVQ LAPVLAIQVT LFPNHGISIG FTNHHVAGDG ATIVKFVRAW
ALLNKFGGDE QFLANEFIPF YDRSVIKDPN GVGMSIWNEM KKYKHMMKMS DVVTPPDKVR
GTFIITRHDI GKLKNLVLTR RPKLTHVTSF TVTCAYVWTC IIKSEAATGE EIDENGMEFF
GCAADCRAQF NPPLPPSYFG NALVGYVART RQVDLAGKEG FTIAVELIGE AIRKRMKDEE
WILSGSWFKE YDKVDAKRSL SVAGSPKLDL YAADFGWGRP EKLEFVSIDN DDGISMSLSK
SKDSDGDLEI GLSLSKTRMN AFAAMFTHGI SFL
