(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 61.
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};
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   STRING; 3702.AT4G26420.1; -.
DR   PaxDb; F4JUY5; -.
DR   PRIDE; F4JUY5; -.
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; ENOG410IIJ3; Eukaryota.
DR   eggNOG; ENOG410Y96G; LUCA.
DR   HOGENOM; HOG000238197; -.
DR   InParanoid; F4JUY5; -.
DR   KO; K18885; -.
DR   OMA; EYRVSAM; -.
DR   OrthoDB; 689338at2759; -.
DR   BioCyc; MetaCyc:AT4G26420-MONOMER; -.
DR   BRENDA; 2.1.1.275; 399.
DR   PRO; PR:F4JUY5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JUY5; baseline and differential.
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   InterPro; IPR005299; MeTrfase_7.
DR   InterPro; IPR042086; MeTrfase_capping.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR31009; PTHR31009; 1.
DR   Pfam; PF03492; Methyltransf_7; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
DR   PRODOM; F4JUY5.
DR   SWISS-2DPAGE; F4JUY5.
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   REGION          63..64
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250"
FT   REGION          136..138
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250"
FT   REGION          153..155
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250"
FT   METAL           175
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           179
FT                   /note="Magnesium; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   METAL           265
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           266
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           268
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           269
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /note="S-adenosyl-L-methionine"
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
//

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