PXMT2_ARATH
ID PXMT2_ARATH Reviewed; 353 AA.
AC Q9C9M2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Paraxanthine methyltransferase 2;
DE EC=2.1.1.- {ECO:0000305};
DE AltName: Full=SABATH methyltransferase PXMT2 {ECO:0000305};
GN OrderedLocusNames=At1g66690 {ECO:0000312|Araport:AT1G66690};
GN ORFNames=F4N21.17 {ECO:0000312|EMBL:AAG60089.1};
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 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).
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 -!- INDUCTION: Induced in the presence of the herbivory P.xylostella
CC larvae. {ECO:0000269|PubMed:14617060}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
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DR EMBL; AC013288; AAG60089.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34545.1; -; Genomic_DNA.
DR RefSeq; NP_176842.1; NM_105340.2.
DR AlphaFoldDB; Q9C9M2; -.
DR SMR; Q9C9M2; -.
DR STRING; 3702.AT1G66690.1; -.
DR PaxDb; Q9C9M2; -.
DR PRIDE; Q9C9M2; -.
DR ProteomicsDB; 226463; -.
DR EnsemblPlants; AT1G66690.1; AT1G66690.1; AT1G66690.
DR GeneID; 842987; -.
DR Gramene; AT1G66690.1; AT1G66690.1; AT1G66690.
DR KEGG; ath:AT1G66690; -.
DR Araport; AT1G66690; -.
DR TAIR; locus:2033414; AT1G66690.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR HOGENOM; CLU_019628_1_0_1; -.
DR InParanoid; Q9C9M2; -.
DR OMA; RINDFNT; -.
DR OrthoDB; 689338at2759; -.
DR PhylomeDB; Q9C9M2; -.
DR BioCyc; ARA:AT1G66690-MON; -.
DR PRO; PR:Q9C9M2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9M2; 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:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0080027; P:response to herbivore; 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 Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..353
FT /note="Paraxanthine methyltransferase 2"
FT /id="PRO_0000440975"
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"
SQ SEQUENCE 353 AA; 39923 MW; 02C0C479013F8950 CRC64;
MTTTQDWIMI GGYGPESYNQ QSSYQRALLE AAKDKMTEAI SANLDLDLIS NRFIVADFGC
ASGPNTFVAV QNIIDAVEEK YLRETGQNPE DNIEFQVLFN DLRINDFNTL FQTLPPGRRY
FSAGVPGSFF NRVLPKQSFH IAVMSYAFLF TSKIPKGIMD RDSPLWNKDM QCTGFNPAVK
KAYLEQYSID TKNLLDARAE ELMPGGLMLL LGSCMRDGVK MSETLKGTVM DFIGESLNDL
AQKGVTEQEK VDTFKTSIYF AEQGEIRQII EENGKFTIEA FEDIIHSKNE FPLDPKTLAI
SFKALYGAFI SAHFGIEVMR KAFELVEVKA REQISRLHKV KPGMQYLIVL RKN
