PMAT2_ARATH
ID PMAT2_ARATH Reviewed; 451 AA.
AC Q9LRQ8;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Phenolic glucoside malonyltransferase 2;
DE EC=2.3.1.- {ECO:0000269|PubMed:20626660};
GN Name=PMAT2; OrderedLocusNames=At3g29670; ORFNames=MOD1_4;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Malonyltransferase acting on xenobiotic glucosides. Has
CC activity toward 2-Naphthol glucoside (2NAG), 1-Naphthol glucoside
CC (1NAG), kaempferol 7-O-glucoside, hydroxycoumarin glucosides and
CC phenol-glucosides, but not toward kaempferol 3-O-glucoside or daidzin.
CC Prefers phenol glucosides rather than naphtol glucosides. In vivo,
CC seems to be involved in the malonylation of 4-methylumbelliferone
CC glucoside or 4-nitrophenyl glucoside while PMAT1 would be involved in
CC the malonylation of 2-Naphthol glucoside.
CC {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 -!- INDUCTION: Up-regulated by high sucrose and by low phosphate stresses.
CC {ECO:0000269|PubMed:17425720}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. Phenolic
CC glucoside malonyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AB028618; BAB02518.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77599.1; -; Genomic_DNA.
DR EMBL; AK118746; BAC43339.1; -; mRNA.
DR EMBL; BT006030; AAP04017.1; -; mRNA.
DR RefSeq; NP_189609.1; NM_113889.3.
DR AlphaFoldDB; Q9LRQ8; -.
DR SMR; Q9LRQ8; -.
DR STRING; 3702.AT3G29670.1; -.
DR PaxDb; Q9LRQ8; -.
DR PRIDE; Q9LRQ8; -.
DR ProteomicsDB; 234936; -.
DR DNASU; 822645; -.
DR EnsemblPlants; AT3G29670.1; AT3G29670.1; AT3G29670.
DR GeneID; 822645; -.
DR Gramene; AT3G29670.1; AT3G29670.1; AT3G29670.
DR KEGG; ath:AT3G29670; -.
DR Araport; AT3G29670; -.
DR TAIR; locus:2091798; AT3G29670.
DR eggNOG; ENOG502QPXT; Eukaryota.
DR HOGENOM; CLU_014546_7_0_1; -.
DR InParanoid; Q9LRQ8; -.
DR OMA; RWVERIT; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9LRQ8; -.
DR BioCyc; ARA:AT3G29670-MON; -.
DR BioCyc; MetaCyc:AT3G29670-MON; -.
DR PRO; PR:Q9LRQ8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRQ8; baseline and differential.
DR Genevisible; Q9LRQ8; AT.
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 Acyltransferase; Detoxification; Reference proteome; Transferase.
FT CHAIN 1..451
FT /note="Phenolic glucoside malonyltransferase 2"
FT /id="PRO_0000419543"
FT MOTIF 165..169
FT /note="HXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT MOTIF 395..399
FT /note="DFGWG motif"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT BINDING 270
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT BINDING 272..273
FT /ligand="malonyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57384"
FT /evidence="ECO:0000250|UniProtKB:Q589Y0"
SQ SEQUENCE 451 AA; 50217 MW; 3CAFAF2E525FEFC1 CRC64;
MTLHVIETAR VTPTDYSVIN SANLHKLPLT FFDLPWLLFQ PVKRVFFYEL TESTRDHFHS
IILPKLKDSL SLILRNYLPL TGHITWEPNE PKPSIIVSEN GVVLVTIAES DADFSHLSGY
GQRPLSELHA LVPKLPVSDD SATAFSIQIT LFPNQGFSIG VAAHHAVLDG KTSSTFIKAW
AQICKQELQS MPENLTPSYD RSLIKYPTYL DEKMIELVRS LKEDQTNIRS LTSLPSSKLG
DDVVLATLVL SRADIERLRE QVKNVSPSLH LSTFVIAYAY AWTCFVKARG GNKDRSVSLL
FVGDFRDRLD PKLPGTYFGN CMIPVGCYNR KAAEFMEEKG FVTAAEIISD LVKGLSSRKI
ETIADTFVEG FSFQSWSTQF GTIAGSTRLG VYEADFGWGR PVKVDIVSID QGEAIAMAER
RDESGGVEIG MCLKKTEMDS VVSFFNNGLH S
