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Gibberellic acid methyltransferase 2 (Gibberellin A(4) carboxyl methyltransferase) (EC 2.1.1.276)

 GAMT2_ARATH             Reviewed;         387 AA.
Q5XF78; Q9FMA2;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
25-APR-2018, entry version 84.
RecName: Full=Gibberellic acid methyltransferase 2;
AltName: Full=Gibberellin A(4) carboxyl methyltransferase;
EC=2.1.1.276;
Name=GAMT2; OrderedLocusNames=At5g56300; ORFNames=MCD7.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[4]
INDUCTION.
PubMed=14617060; DOI=10.1046/j.1365-313X.2003.01902.x;
Chen F., D'Auria J.C., Tholl D., Ross J.R., Gershenzon J., Noel J.P.,
Pichersky E.;
"An Arabidopsis thaliana gene for methylsalicylate biosynthesis,
identified by a biochemical genomics approach, has a role in
defense.";
Plant J. 36:577-588(2003).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=17220201; DOI=10.1105/tpc.106.044602;
Varbanova M., Yamaguchi S., Yang Y., McKelvey K., Hanada A.,
Borochov R., Yu F., Jikumaru Y., Ross J., Cortes D., Ma C.J.,
Noel J.P., Mander L., Shulaev V., Kamiya Y., Rodermel S., Weiss D.,
Pichersky E.;
"Methylation of gibberellins by Arabidopsis GAMT1 and GAMT2.";
Plant Cell 19:32-45(2007).
-!- FUNCTION: Methylates the carboxyl group of several gibberellins
(GAs). Substrate preference is GA4 > GA34 > GA9 > GA3 > GA1 > GA51
> GA20. No activity with diterpenes abietic acid and ent-kaurenoic
acid. {ECO:0000269|PubMed:17220201}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + gibberellin A(4) =
S-adenosyl-L-homocysteine + methyl gibberellin A(4).
{ECO:0000269|PubMed:17220201}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Down-regulated by Zn(2+), Cu(2+) and Fe(3+). No
effect of K(+), NH(4+), Na(+), Ca(2+), Mg(2+), Mn(2+) and Fe(2+).
{ECO:0000269|PubMed:17220201}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.9 uM for GA4 {ECO:0000269|PubMed:17220201};
KM=1.9 uM for GA9 {ECO:0000269|PubMed:17220201};
Note=kcat is 0.0015 sec(-1) for GA4. kcat is 0.0018 sec(-1) for
GA9.;
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:17220201};
-!- TISSUE SPECIFICITY: Expressed in siliques and germinating seeds.
Not detected in leaves, stems, flowers and roots.
{ECO:0000269|PubMed:17220201}.
-!- DEVELOPMENTAL STAGE: Expression begins at early stages of silique
development, peaks in the second half of this process and
decreases after the start of desiccation.
{ECO:0000269|PubMed:17220201}.
-!- INDUCTION: Up-regulated by alamethicin, but not by herbivory.
{ECO:0000269|PubMed:14617060}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, even in gamt1 and
gamt2 double mutants. {ECO:0000269|PubMed:17220201}.
-!- MISCELLANEOUS: Overexpression of GAMT2 results in dwarf phenotype.
{ECO:0000305|PubMed:17220201}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
methyltransferase family. SABATH subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB11257.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB009049; BAB11257.1; ALT_INIT; Genomic_DNA.
EMBL; CP002688; AED96746.1; -; Genomic_DNA.
EMBL; BT015738; AAU84675.1; -; mRNA.
EMBL; BT020177; AAV43779.1; -; mRNA.
RefSeq; NP_200441.2; NM_125013.3.
UniGene; At.29396; -.
ProteinModelPortal; Q5XF78; -.
SMR; Q5XF78; -.
STRING; 3702.AT5G56300.1; -.
PaxDb; Q5XF78; -.
DNASU; 835729; -.
EnsemblPlants; AT5G56300.1; AT5G56300.1; AT5G56300.
GeneID; 835729; -.
Gramene; AT5G56300.1; AT5G56300.1; AT5G56300.
KEGG; ath:AT5G56300; -.
Araport; AT5G56300; -.
TAIR; locus:2161008; AT5G56300.
eggNOG; ENOG410IJ2U; Eukaryota.
eggNOG; ENOG4112BHH; LUCA.
HOGENOM; HOG000238197; -.
InParanoid; Q5XF78; -.
KO; K18886; -.
OMA; TRAKHPF; -.
OrthoDB; EOG09360HY5; -.
PhylomeDB; Q5XF78; -.
BioCyc; MetaCyc:AT5G56300-MONOMER; -.
BRENDA; 2.1.1.276; 399.
PRO; PR:Q5XF78; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q5XF78; baseline and differential.
Genevisible; Q5XF78; AT.
GO; GO:0102118; F:gibberellin A4 carboxyl methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0010341; F:gibberellin carboxyl-O-methyltransferase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:TAIR.
InterPro; IPR005299; MeTrfase_7.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR31009; PTHR31009; 1.
Pfam; PF03492; Methyltransf_7; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Magnesium; Metal-binding; Methyltransferase;
Reference proteome; S-adenosyl-L-methionine; Transferase.
CHAIN 1 387 Gibberellic acid methyltransferase 2.
/FTId=PRO_0000422311.
REGION 73 74 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 146 148 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 163 165 S-adenosyl-L-methionine binding.
{ECO:0000250}.
METAL 185 185 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 275 275 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 276 276 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 278 278 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 279 279 Magnesium. {ECO:0000250}.
BINDING 79 79 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 113 113 S-adenosyl-L-methionine. {ECO:0000250}.
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


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