PXMT1_ARATH
ID PXMT1_ARATH Reviewed; 353 AA.
AC Q9C9M3; F4HPZ7; Q8LGA6; Q941F2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Paraxanthine methyltransferase 1 {ECO:0000303|PubMed:26768601};
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=SABATH methyltransferase PXMT1 {ECO:0000305};
GN Name=PXMT1 {ECO:0000303|PubMed:26768601};
GN OrderedLocusNames=At1g66700 {ECO:0000312|Araport:AT1G66700};
GN ORFNames=F4N21.16 {ECO:0000312|EMBL:AAG60088.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-353 (ISOFORM 1).
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 [6]
RP INDUCTION BY HERBIVORY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=14617060; DOI=10.1046/j.1365-313x.2003.01902.x;
RA Chen F., D'Auria J.C., Tholl D., Ross J.R., Gershenzon J., Noel J.P.,
RA Pichersky E.;
RT "An Arabidopsis thaliana gene for methylsalicylate biosynthesis, identified
RT by a biochemical genomics approach, has a role in defense.";
RL Plant J. 36:577-588(2003).
RN [7]
RP REGULATION BY MIR163 AND ALAMETHICIN.
RC STRAIN=cv. Columbia;
RX PubMed=21602291; DOI=10.1105/tpc.111.083915;
RA Ng D.W., Zhang C., Miller M., Palmer G., Whiteley M., Tholl D., Chen Z.J.;
RT "cis- and trans-Regulation of miR163 and target genes confers natural
RT variation of secondary metabolites in two Arabidopsis species and their
RT allopolyploids.";
RL Plant Cell 23:1729-1740(2011).
RN [8]
RP FUNCTION, REGULATION BY LIGHT AND MIR163, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=26768601; DOI=10.1104/pp.15.01188;
RA Chung P.J., Park B.S., Wang H., Liu J., Jang I.C., Chua N.H.;
RT "Light-inducible miR163 targets PXMT1 transcripts to promote seed
RT germination and primary root elongation in Arabidopsis.";
RL Plant Physiol. 170:1772-1782(2016).
RN [9]
RP FUNCTION, REGULATION BY P.SYRINGAE AND MIR163, AND INDUCTION BY SALICYLIC
RP ACID.
RC STRAIN=cv. Columbia;
RX PubMed=28401908; DOI=10.1038/srep46433;
RA Chow H.T., Ng D.W.-K.;
RT "Regulation of miR163 and its targets in defense against Pseudomonas
RT syringae in Arabidopsis thaliana.";
RL Sci. Rep. 7:46433-46433(2017).
CC -!- FUNCTION: Methyltransferase that may methylate 1,7-paraxanthine
CC (PubMed:26768601). Prevents seed germination and modulates root
CC architecture during early seedlings development (PubMed:26768601).
CC Plays a minor role in defense responses toward pathogenic bacteria
CC (e.g. P.syringae) (PubMed:28401908). {ECO:0000269|PubMed:26768601,
CC ECO:0000269|PubMed:28401908, ECO:0000303|PubMed:26768601}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FLN8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C9M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C9M3-2; Sequence=VSP_059017;
CC -!- DEVELOPMENTAL STAGE: During seed germination, predominantly expressed
CC in the radicle and, to a lower extent, in hypocotyls.
CC {ECO:0000269|PubMed:26768601}.
CC -!- INDUCTION: Induced in the presence of the herbivory P.xylostella larvae
CC (PubMed:14617060). Silenced by miR163 (PubMed:21602291,
CC PubMed:26768601, PubMed:28401908). Down-regulated during seedling
CC deetiolation and seed germination via light-induced silencing mediated
CC by miR163 (PubMed:21602291, PubMed:26768601). Accumulates in etiolated
CC seedlings (PubMed:26768601). Induced by the fungal elicitor alamethicin
CC (PubMed:21602291). Slightly up-regulated by P.syringae. Induced by
CC exogenous salicylic acid (SA) (PubMed:28401908).
CC {ECO:0000269|PubMed:14617060, ECO:0000269|PubMed:21602291,
CC ECO:0000269|PubMed:26768601, ECO:0000269|PubMed:28401908}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK97663.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM67278.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013288; AAG60088.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34546.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34547.1; -; Genomic_DNA.
DR EMBL; BX816624; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY084375; AAM67278.1; ALT_INIT; mRNA.
DR EMBL; AY052192; AAK97663.1; ALT_INIT; mRNA.
DR EMBL; AY143812; AAN28751.1; -; mRNA.
DR RefSeq; NP_564881.3; NM_105341.5. [Q9C9M3-1]
DR RefSeq; NP_974096.1; NM_202367.3. [Q9C9M3-2]
DR AlphaFoldDB; Q9C9M3; -.
DR SMR; Q9C9M3; -.
DR STRING; 3702.AT1G66700.1; -.
DR PaxDb; Q9C9M3; -.
DR PRIDE; Q9C9M3; -.
DR ProteomicsDB; 224795; -. [Q9C9M3-1]
DR DNASU; 842988; -.
DR EnsemblPlants; AT1G66700.1; AT1G66700.1; AT1G66700. [Q9C9M3-1]
DR EnsemblPlants; AT1G66700.3; AT1G66700.3; AT1G66700. [Q9C9M3-2]
DR GeneID; 842988; -.
DR Gramene; AT1G66700.1; AT1G66700.1; AT1G66700. [Q9C9M3-1]
DR Gramene; AT1G66700.3; AT1G66700.3; AT1G66700. [Q9C9M3-2]
DR KEGG; ath:AT1G66700; -.
DR Araport; AT1G66700; -.
DR TAIR; locus:2033409; AT1G66700.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR InParanoid; Q9C9M3; -.
DR OMA; HFGVEVM; -.
DR PhylomeDB; Q9C9M3; -.
DR BioCyc; ARA:AT1G66700-MON; -.
DR PRO; PR:Q9C9M3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9M3; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IEP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IMP:UniProtKB.
DR GO; GO:1900140; P:regulation of seedling development; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Magnesium; Metal-binding;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..353
FT /note="Paraxanthine methyltransferase 1"
FT /id="PRO_0000440974"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 59..60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 99..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 128..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 145..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 146..150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT VAR_SEQ 244..352
FT /note="GVTEQEKVDTFRTSIYFAEQGEIRQIIEENGKFTIEAFEDIIHAKNEFPFDP
FT KTLAISFKAFYGAFISAHFGVEVMRKAFELVEVKAREQISRLHNSKPGMQYLIVLRK
FT -> VHNLIVIVLYNCIST (in isoform 2)"
FT /id="VSP_059017"
FT CONFLICT 39
FT /note="A -> V (in Ref. 4; AAM67278)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="C -> Y (in Ref. 3; BX816624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39780 MW; 2A13D873864FAD20 CRC64;
MTTTPDWIMI GGDGPESYNQ QSSYQRALLE ATKDKMTKAI SANLDLDLIS NRFIVADFGC
ASGPNTFVAV QNIIDAVEEK YRRETGQNPA DNIEFQVLFN DFSLNDFNTL FQTLPPGRRY
FSAGVPGSFF ERVLPKESFH IGVMSYAFHF TSKIPKGIMD RDSPLWNKDM QCTGFNPAVK
KAYLDQYSID TKILLDARAE ELVPGGLMLL LGSCLRDGVK MSETPKGTVM DFIGESLSDL
AKQGVTEQEK VDTFRTSIYF AEQGEIRQII EENGKFTIEA FEDIIHAKNE FPFDPKTLAI
SFKAFYGAFI SAHFGVEVMR KAFELVEVKA REQISRLHNS KPGMQYLIVL RKN
