PXMT3_ARATH
ID PXMT3_ARATH Reviewed; 352 AA.
AC Q9C9M4;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Paraxanthine methyltransferase 3;
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=SABATH methyltransferase PXMT3 {ECO:0000305};
GN OrderedLocusNames=At1g66720 {ECO:0000312|Araport:AT1G66720};
GN ORFNames=F4N21.15 {ECO:0000312|EMBL:AAG60084.1};
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 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).
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 -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
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DR EMBL; AC013288; AAG60084.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34548.1; -; Genomic_DNA.
DR RefSeq; NP_176844.1; NM_105342.1.
DR AlphaFoldDB; Q9C9M4; -.
DR SMR; Q9C9M4; -.
DR STRING; 3702.AT1G66720.1; -.
DR PaxDb; Q9C9M4; -.
DR PRIDE; Q9C9M4; -.
DR EnsemblPlants; AT1G66720.1; AT1G66720.1; AT1G66720.
DR GeneID; 842990; -.
DR Gramene; AT1G66720.1; AT1G66720.1; AT1G66720.
DR KEGG; ath:AT1G66720; -.
DR Araport; AT1G66720; -.
DR TAIR; locus:2033389; AT1G66720.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR HOGENOM; CLU_019628_1_0_1; -.
DR InParanoid; Q9C9M4; -.
DR OMA; KMSETYR; -.
DR OrthoDB; 689338at2759; -.
DR PhylomeDB; Q9C9M4; -.
DR BioCyc; ARA:AT1G66720-MON; -.
DR PRO; PR:Q9C9M4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9M4; 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:0032259; P:methylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..352
FT /note="Paraxanthine methyltransferase 3"
FT /id="PRO_0000440976"
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 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
SQ SEQUENCE 352 AA; 39290 MW; F0C614F98D6A063F CRC64;
MSPTPEWVMV GGEGPESYKQ HSSYQRDLLK AAKDKINAVI STNLSLNLIS NRFSVADFGC
ASGPNTFVAV QNIIDAVEEK YLRETGQNPD DNIEFQVLFN DLSNNDFNTL FQGLPSGRRY
YSAAIPGSFF DRVLPKHSIH IGVMNYAFQF TSKIPKGISD RNSPLWNRDM HCTGFNNKVK
KAYLDQFSLD SKNILDARAE ELVPEGLMLL LGSCLRDGIK MSETYRGIVL DLIGASLNDL
AQQGVIEKDK VESFNITLYI AEEGELRQII EENGKFTIEA FEDIIQPNGE SLDPKILAVS
LKSAFGGILS AHFGAEAMMK AFELVEAKAH QEFSRLQNAK PTMQYLIVLR KN
