FAMT_ARATH
ID FAMT_ARATH Reviewed; 348 AA.
AC Q9FYC4; Q949P9;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Farnesoic acid carboxyl-O-methyltransferase {ECO:0000303|PubMed:16165084};
DE EC=2.1.1.325 {ECO:0000269|PubMed:16165084};
DE AltName: Full=SABATH methyltransferase FAMT {ECO:0000305};
GN Name=FAMT {ECO:0000303|PubMed:16165084};
GN OrderedLocusNames=At3g44860 {ECO:0000312|Araport:AT3G44860};
GN ORFNames=F28D10.50 {ECO:0000312|EMBL:CAC03536.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY
RP WOUNDING; SALICYLIC ACID; JASMONIC ACID AND ALAMETHICIN, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16165084; DOI=10.1016/j.abb.2005.08.006;
RA Yang Y., Yuan J.S., Ross J., Noel J.P., Pichersky E., Chen F.;
RT "An Arabidopsis thaliana methyltransferase capable of methylating farnesoic
RT acid.";
RL Arch. Biochem. Biophys. 448:123-132(2006).
CC -!- FUNCTION: May catalyze the production of the insect juvenile hormone
CC methyl farnesoate (MeFA) to trigger defense against insect herbivory.
CC {ECO:0000303|PubMed:16165084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesoate + S-adenosyl-L-methionine = methyl (2E,6E)-
CC farnesoate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43700,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:80535,
CC ChEBI:CHEBI:83276; EC=2.1.1.325;
CC Evidence={ECO:0000269|PubMed:16165084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=juvenile hormone III carboxylate + S-adenosyl-L-methionine =
CC juvenile hormone III + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43720, ChEBI:CHEBI:27493, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:83274; EC=2.1.1.325;
CC Evidence={ECO:0000269|PubMed:16165084};
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 -!- ACTIVITY REGULATION: Activated by Mn(2+) ions. Strongly inhibited by
CC Cu(2+), Zn(2+), Fe(3+) and Fe(2+) ions. Moderately inhibited by Na(+)
CC and Ca(2+) ions. Rapidly degraded at temperatures above 40 degrees
CC Celsius. {ECO:0000269|PubMed:16165084}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41 uM for farnesoic acid {ECO:0000269|PubMed:16165084};
CC KM=71 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16165084};
CC Note=kcat is 0.004 sec(-1) with farnesoic acid as substrate.
CC {ECO:0000269|PubMed:16165084};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:16165084};
CC -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:16165084}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FLN8}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and, at very low levels,
CC in roots, stems, flowers and siliques. {ECO:0000269|PubMed:16165084}.
CC -!- INDUCTION: Induced in the presence of the herbivory P.xylostella larvae
CC (PubMed:14617060). Accumulates slighty in response to wounding and to
CC several defense responses-inducing compounds including salicylic acid
CC (SA), jasmonic acid (MeJA) and alamethicin (Ala), an antibiotic peptide
CC of fungal origin (PubMed:16165084). {ECO:0000269|PubMed:14617060,
CC ECO:0000269|PubMed:16165084}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
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DR EMBL; AL391254; CAC03536.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77962.1; -; Genomic_DNA.
DR EMBL; AY050969; AAK93646.1; -; mRNA.
DR EMBL; AY150400; AAN12945.1; -; mRNA.
DR PIR; T51783; T51783.
DR RefSeq; NP_190072.1; NM_114355.3.
DR AlphaFoldDB; Q9FYC4; -.
DR SMR; Q9FYC4; -.
DR STRING; 3702.AT3G44860.1; -.
DR PaxDb; Q9FYC4; -.
DR PRIDE; Q9FYC4; -.
DR ProteomicsDB; 222378; -.
DR DNASU; 823620; -.
DR EnsemblPlants; AT3G44860.1; AT3G44860.1; AT3G44860.
DR GeneID; 823620; -.
DR Gramene; AT3G44860.1; AT3G44860.1; AT3G44860.
DR KEGG; ath:AT3G44860; -.
DR Araport; AT3G44860; -.
DR TAIR; locus:2082112; AT3G44860.
DR eggNOG; ENOG502QUIN; Eukaryota.
DR HOGENOM; CLU_019628_1_0_1; -.
DR InParanoid; Q9FYC4; -.
DR OMA; IMFDCMG; -.
DR OrthoDB; 689338at2759; -.
DR PhylomeDB; Q9FYC4; -.
DR BioCyc; ARA:AT3G44860-MON; -.
DR BioCyc; MetaCyc:AT3G44860-MON; -.
DR PRO; PR:Q9FYC4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FYC4; baseline and differential.
DR GO; GO:0019010; F:farnesoic acid O-methyltransferase activity; IDA:TAIR.
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 GO; GO:0009753; P:response to jasmonic acid; 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 GO; GO:0009611; P:response to wounding; 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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..348
FT /note="Farnesoic acid carboxyl-O-methyltransferase"
FT /id="PRO_0000440977"
FT BINDING 16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 19..23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 57..58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 94..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 123..125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 140..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 141..145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT CONFLICT 149
FT /note="V -> F (in Ref. 3; AAK93646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38515 MW; 30DD9B982603E7F7 CRC64;
MSTSFTMIGG EGPNSYREHS KYQGALVIAA KEKINEAIST KLDIDFTSNL VNIADFGCSS
GPNTFTAVQT LIDAVENKYK KESNIEGIEF QVFFNDSSNN DFNTLFKTLP PARLYFASGV
PGSFFGRVLP KNSLHVGVSS YSLHFVSKVP KEIKDRDSLV WNKDIHCSGS SKEVVKLYLG
QYKIDVGSFL TARAQELVSG GLLLLLGSCR PTGVQMFETV EGMMIDFIGS SLNEIANQGL
IDQQKLDTFK LPIYAPNVDE LKQIIEDNKC FTIEAFEKIS HAKGEYPLDP EYLTSAFKVT
VGGSVASLFG QDGMEKTYEL VKEKTQEMLP QIAKAKPGMQ YLIVLRRN
