PMAT1_ARATH
ID PMAT1_ARATH Reviewed; 469 AA.
AC Q940Z5; Q9FID3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Phenolic glucoside malonyltransferase 1;
DE EC=2.3.1.- {ECO:0000269|PubMed:20626660};
DE EC=2.3.1.116 {ECO:0000269|PubMed:20626660};
GN Name=PMAT1; OrderedLocusNames=At5g39050; ORFNames=MXF12.60;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=17425720; DOI=10.1111/j.1365-313x.2007.03079.x;
RA Luo J., Nishiyama Y., Fuell C., Taguchi G., Elliott K., Hill L., Tanaka Y.,
RA Kitayama M., Yamazaki M., Bailey P., Parr A., Michael A.J., Saito K.,
RA Martin C.;
RT "Convergent evolution in the BAHD family of acyl transferases:
RT identification and characterization of anthocyanin acyl transferases from
RT Arabidopsis thaliana.";
RL Plant J. 50:678-695(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20626660; DOI=10.1111/j.1365-313x.2010.04298.x;
RA Taguchi G., Ubukata T., Nozue H., Kobayashi Y., Takahi M., Yamamoto H.,
RA Hayashida N.;
RT "Malonylation is a key reaction in the metabolism of xenobiotic phenolic
RT glucosides in Arabidopsis and tobacco.";
RL Plant J. 63:1031-1041(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Malonyltransferase acting on xenobiotic glucosides. Has
CC activity toward 2-Naphthol glucoside (2NAG), 1-Naphthol glucoside
CC (1NAG), kaempferol 7-O-glucoside, kaempferol 3-O-glucoside,
CC hydroxycoumarin glucosides, phenol-glucosides and isoflavone glucoside
CC (daidzin), but not toward 4-coumaroyl glucoside, kaempferol 3,7-O-
CC diglucoside, salicylic acid glucoside and phlorizin. In vivo, seems to
CC be involved in the malonylation of 2-Naphthol glucoside while PMAT2
CC would be involved in the malonylation of 4-methylumbelliferone
CC glucoside or 4-nitrophenyl glucoside. {ECO:0000269|PubMed:20626660}.
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:20626660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20086;
CC Evidence={ECO:0000269|PubMed:20626660};
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:20626660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58797;
CC Evidence={ECO:0000269|PubMed:20626660};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=85 uM for 2-Naphthol glucoside {ECO:0000269|PubMed:20626660};
CC KM=160 uM for 1-Naphthol glucoside {ECO:0000269|PubMed:20626660};
CC KM=31 uM for kaempferol 7-O-glucoside {ECO:0000269|PubMed:20626660};
CC KM=1.6 mM for 4-nitrophenyl glucoside {ECO:0000269|PubMed:20626660};
CC KM=0.55 mM for 4-methylumbelliferone glucoside
CC {ECO:0000269|PubMed:20626660};
CC KM=2.3 uM for malonyl-CoA {ECO:0000269|PubMed:20626660};
CC Note=kcat is 40 sec(-1) for 2-Naphthol glucoside. kcat is 46 sec(-1)
CC for 1-Naphthol glucoside. kcat is 33 sec(-1) for kaempferol 7-O-
CC glucoside. kcat is 120 sec(-1) for 4-nitrophenyl glucoside. kcat is
CC 19 sec(-1) for 4-methylumbelliferone glucoside. kcat is 23 sec(-1)
CC for malonyl-CoA.;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but no malonylation of
CC glucosides. {ECO:0000269|PubMed:20626660}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. Phenolic
CC glucoside malonyltransferase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016892; BAB10829.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94391.1; -; Genomic_DNA.
DR EMBL; AY052335; AAK96528.1; -; mRNA.
DR EMBL; BT002269; AAN72280.1; -; mRNA.
DR RefSeq; NP_568561.4; NM_123267.6.
DR AlphaFoldDB; Q940Z5; -.
DR SMR; Q940Z5; -.
DR STRING; 3702.AT5G39050.1; -.
DR iPTMnet; Q940Z5; -.
DR PaxDb; Q940Z5; -.
DR PRIDE; Q940Z5; -.
DR ProteomicsDB; 234935; -.
DR EnsemblPlants; AT5G39050.1; AT5G39050.1; AT5G39050.
DR GeneID; 833897; -.
DR Gramene; AT5G39050.1; AT5G39050.1; AT5G39050.
DR KEGG; ath:AT5G39050; -.
DR Araport; AT5G39050; -.
DR TAIR; locus:2177172; AT5G39050.
DR eggNOG; ENOG502QPXT; Eukaryota.
DR HOGENOM; CLU_014546_7_0_1; -.
DR InParanoid; Q940Z5; -.
DR OMA; FWANACK; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q940Z5; -.
DR BioCyc; ARA:AT5G39050-MON; -.
DR BioCyc; MetaCyc:AT5G39050-MON; -.
DR PRO; PR:Q940Z5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q940Z5; baseline and differential.
DR Genevisible; Q940Z5; AT.
DR GO; GO:0047165; F:flavonol-3-O-beta-glucoside O-malonyltransferase activity; IEA:RHEA.
DR GO; GO:0050736; F:O-malonyltransferase activity; IDA:TAIR.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Detoxification; Reference proteome;
KW Transferase.
FT CHAIN 1..469
FT /note="Phenolic glucoside malonyltransferase 1"
FT /id="PRO_0000419542"
FT MOTIF 169..173
FT /note="HXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT MOTIF 413..417
FT /note="DFGWG motif"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT ACT_SITE 413
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT BINDING 291..292
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 469 AA; 51765 MW; DA534E4FF4ADEE9F CRC64;
MVNEEMESSL KVIDVARVTP SNSDSSESLT LPLTFFDLLW YKLHAVERVI FYKLTDASRP
FFDSVIVPNL KTSLSSSLSH YLPLAGKLVW EPLDPKPKIV YTPNDAVSFT VAESNADFSR
LTGKEPFPTT ELYPLVPELH VSDDSASAVS FQVTLFPNQG FCISVNAHHA VLDGKTTTNF
LKSWARTCKN QDSFLPQDLI PVYDRTVIKD PMDLDTKILN AWHRVAKVFT GGKEPENPKS
LKLLWSPEIG PDVFRYTLNL TREDIQKLRE RLKKESSSSS VSSSPKELRL STFVIVYSYA
LTCLIKARGG DPSRPVGYGF AVDCRSLMVP PVPSSYFGNC VSACFKMSLT AETFMSEEGF
LAAARMVSDS VEALDENVAL KIPEILEGFT TLSPGTQVLS VAGSTRFGVY GLDFGWGRPE
KVVVVSIDQG EAISFAESRD GSGGVELGFS LKKHEMDVLV DLLHKGLEN
