GAMT2_ARATH
ID GAMT2_ARATH Reviewed; 387 AA.
AC Q5XF78; Q9FMA2;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Gibberellic acid methyltransferase 2;
DE AltName: Full=Gibberellin A(4) carboxyl methyltransferase;
DE EC=2.1.1.276;
GN Name=GAMT2; OrderedLocusNames=At5g56300; ORFNames=MCD7.2;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
RA Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION.
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, 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 GA4 > GA34 > GA9 > GA3 > GA1 > GA51 > GA20. No
CC activity with diterpenes abietic acid and ent-kaurenoic acid.
CC {ECO:0000269|PubMed:17220201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gibberellin A4 + S-adenosyl-L-methionine = O-methyl
CC gibberellin A4 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36107,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73251,
CC ChEBI:CHEBI:73252; EC=2.1.1.276;
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: Down-regulated by Zn(2+), Cu(2+) and Fe(3+). No
CC effect of K(+), NH(4+), Na(+), Ca(2+), Mg(2+), Mn(2+) and Fe(2+).
CC {ECO:0000269|PubMed:17220201}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for GA4 {ECO:0000269|PubMed:17220201};
CC KM=1.9 uM for GA9 {ECO:0000269|PubMed:17220201};
CC Note=kcat is 0.0015 sec(-1) for GA4. kcat is 0.0018 sec(-1) for GA9.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17220201};
CC -!- TISSUE SPECIFICITY: Expressed in siliques and germinating seeds. Not
CC detected in leaves, stems, flowers and roots.
CC {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 -!- INDUCTION: Up-regulated by alamethicin, but not by herbivory.
CC {ECO:0000269|PubMed:14617060}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, even in gamt1 and gamt2
CC double mutants. {ECO:0000269|PubMed:17220201}.
CC -!- MISCELLANEOUS: Overexpression of GAMT2 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=BAB11257.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB009049; BAB11257.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED96746.1; -; Genomic_DNA.
DR EMBL; BT015738; AAU84675.1; -; mRNA.
DR EMBL; BT020177; AAV43779.1; -; mRNA.
DR RefSeq; NP_200441.2; NM_125013.3.
DR AlphaFoldDB; Q5XF78; -.
DR SMR; Q5XF78; -.
DR STRING; 3702.AT5G56300.1; -.
DR PaxDb; Q5XF78; -.
DR PRIDE; Q5XF78; -.
DR ProteomicsDB; 248557; -.
DR DNASU; 835729; -.
DR EnsemblPlants; AT5G56300.1; AT5G56300.1; AT5G56300.
DR GeneID; 835729; -.
DR Gramene; AT5G56300.1; AT5G56300.1; AT5G56300.
DR KEGG; ath:AT5G56300; -.
DR Araport; AT5G56300; -.
DR TAIR; locus:2161008; AT5G56300.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_1_1_1; -.
DR InParanoid; Q5XF78; -.
DR OMA; RAKHPFT; -.
DR OrthoDB; 689338at2759; -.
DR PhylomeDB; Q5XF78; -.
DR BioCyc; MetaCyc:AT5G56300-MON; -.
DR BRENDA; 2.1.1.276; 399.
DR PRO; PR:Q5XF78; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5XF78; baseline and differential.
DR Genevisible; Q5XF78; AT.
DR GO; GO:0102118; F:gibberellin A4 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 Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..387
FT /note="Gibberellic acid methyltransferase 2"
FT /id="PRO_0000422311"
FT BINDING 73..74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 146..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163..165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 43349 MW; 22B310B82CDEF3CD CRC64;
MESPSLPMTA KDWTTTSLHR VFAMQGGEDD LSYVNNSDSQ ALAITLSKPI LISSLQSIKL
FSDQTPIKIT DLGCATGSNT FTTVDTVVET LQRRYTARCG GGGSPEFEAF FCDLPSNDFN
MLFKLLAEKQ KVDSPAKYFA GGVAGSFYDR LFPRGTIHVA VSLSALHWLS QIPEKVLEKE
SRTWNKGKTW IEGAKKEVVE AYAEQSDKDL DDFMSCRKEE MVKGGVLFVL MAGRPSGSSS
QFGDQDTRAK HPFTTTMEQA WQDLIEEGLI DEETRDGFNI PAYMRSPEEV TAGIDRCGGF
KIGKMDFLKI VEYSDEKQEE WKKDPVSYGR ARTNLVQAAI RPMVDAYLGP DLSHELFKRY
ENRVSTNQEF LHITCFYGVV VFSAIRV
