GAMT1_ARATH
ID GAMT1_ARATH Reviewed; 376 AA.
AC F4JUY5; B3H6L1; O65592; Q56Z47;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Gibberellic acid methyltransferase 1;
DE AltName: Full=Gibberellin A(9) O-methyltransferase;
DE EC=2.1.1.275;
GN Name=GAMT1; OrderedLocusNames=At4g26420; ORFNames=M3E9.150;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17220201; DOI=10.1105/tpc.106.044602;
RA Varbanova M., Yamaguchi S., Yang Y., McKelvey K., Hanada A., Borochov R.,
RA Yu F., Jikumaru Y., Ross J., Cortes D., Ma C.J., Noel J.P., Mander L.,
RA Shulaev V., Kamiya Y., Rodermel S., Weiss D., Pichersky E.;
RT "Methylation of gibberellins by Arabidopsis GAMT1 and GAMT2.";
RL Plant Cell 19:32-45(2007).
CC -!- FUNCTION: Methylates the carboxyl group of several gibberellins (GAs).
CC Substrate preference is GA9 > GA20 > GA3 > GA4 > GA34 > GA51 > GA1 >
CC GA19 > GA12. No activity with diterpenes abietic acid and ent-kaurenoic
CC acid. {ECO:0000269|PubMed:17220201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gibberellin A9 + S-adenosyl-L-methionine = O-methyl
CC gibberellin A9 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36119,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73255,
CC ChEBI:CHEBI:73256; EC=2.1.1.275;
CC Evidence={ECO:0000269|PubMed:17220201};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Up-regulated by K(+) and NH(4+), down-regulated by
CC Zn(2+), Cu(2+), Fe(2+) and Fe(3+). {ECO:0000269|PubMed:17220201}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for GA4 {ECO:0000269|PubMed:17220201};
CC KM=15.8 uM for GA9 {ECO:0000269|PubMed:17220201};
CC Note=kcat is 0.01 sec(-1) for GA4. kcat is 0.026 sec(-1) for GA9.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17220201};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JUY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JUY5-2; Sequence=VSP_046497, VSP_046498, VSP_046499;
CC -!- TISSUE SPECIFICITY: Expressed in siliques, developing seeds, anthers
CC and germinating seeds. Not detected in leaves, stems, flowers and
CC roots. {ECO:0000269|PubMed:17220201}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at early stages of silique
CC development, peaks in the second half of this process and decreases
CC after the start of desiccation. {ECO:0000269|PubMed:17220201}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, even in gamt1 and gamt2
CC double mutants. {ECO:0000269|PubMed:17220201}.
CC -!- MISCELLANEOUS: Overexpression of GAMT1 results in dwarf phenotype.
CC {ECO:0000305|PubMed:17220201}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. SABATH subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18228.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79497.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022223; CAA18228.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79497.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85196.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85197.1; -; Genomic_DNA.
DR EMBL; AK221122; BAD95064.1; -; mRNA.
DR PIR; T05062; T05062.
DR RefSeq; NP_001119061.1; NM_001125589.5. [F4JUY5-2]
DR RefSeq; NP_194372.2; NM_118775.3. [F4JUY5-1]
DR AlphaFoldDB; F4JUY5; -.
DR SMR; F4JUY5; -.
DR STRING; 3702.AT4G26420.1; -.
DR PaxDb; F4JUY5; -.
DR PRIDE; F4JUY5; -.
DR ProteomicsDB; 228961; -. [F4JUY5-1]
DR EnsemblPlants; AT4G26420.1; AT4G26420.1; AT4G26420. [F4JUY5-1]
DR EnsemblPlants; AT4G26420.2; AT4G26420.2; AT4G26420. [F4JUY5-2]
DR GeneID; 828748; -.
DR Gramene; AT4G26420.1; AT4G26420.1; AT4G26420. [F4JUY5-1]
DR Gramene; AT4G26420.2; AT4G26420.2; AT4G26420. [F4JUY5-2]
DR KEGG; ath:AT4G26420; -.
DR Araport; AT4G26420; -.
DR TAIR; locus:2131483; AT4G26420.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR InParanoid; F4JUY5; -.
DR OMA; HISHHME; -.
DR OrthoDB; 689338at2759; -.
DR BioCyc; MetaCyc:AT4G26420-MON; -.
DR BRENDA; 2.1.1.275; 399.
DR PRO; PR:F4JUY5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JUY5; baseline.
DR GO; GO:0102117; F:gibberellin A9 carboxyl methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010341; F:gibberellin carboxyl-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; IDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..376
FT /note="Gibberellic acid methyltransferase 1"
FT /id="PRO_0000422310"
FT BINDING 63..64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 136..138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 153..155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046497"
FT VAR_SEQ 258..277
FT /note="GLIEEEKRDGFNIPVYFRTT -> LVKGFNRRGEERWFQHSGVL (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046498"
FT VAR_SEQ 278..376
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046499"
FT CONFLICT 32
FT /note="R -> A (in Ref. 3; BAD95064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41564 MW; 4FD1B43F674B9F88 CRC64;
MESSRSLEHV LSMQGGEDDA SYVKNCYGPA ARLALSKPML TTAINSIKLT EGCSSHLKIA
DLGCAIGDNT FSTVETVVEV LGKKLAVIDG GTEPEMEFEV FFSDLSSNDF NALFRSLDEK
VNGSSRKYFA AGVPGSFYKR LFPKGELHVV VTMSALQWLS QVPEKVMEKG SKSWNKGGVW
IEGAEKEVVE AYAEQADKDL VEFLKCRKEE IVVGGVLFML MGGRPSGSVN QIGDPDSSLK
HPFTTLMDQA WQDLVDEGLI EEEKRDGFNI PVYFRTTEEI AAAIDRCGGF KIEKTENLII
ADHMNGKQEE LMKDPDSYGR DRANYAQAGL KPIVQAYLGP DLTHKLFKRY AVRAAADKEI
LNNCFYHMIA VSAVRV
