METK3_ARATH
ID METK3_ARATH Reviewed; 390 AA.
AC Q9SJL8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=S-adenosylmethionine synthase 3;
DE Short=AdoMet synthase 3;
DE EC=2.5.1.6 {ECO:0000269|PubMed:16365035};
DE AltName: Full=Methionine adenosyltransferase 3;
DE Short=MAT 3;
GN Name=METK3; OrderedLocusNames=At2g36880; ORFNames=T1J8.6;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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 FUNCTION, MUTAGENESIS OF ASP-167, AND PATHWAY.
RX PubMed=12087191; DOI=10.1266/ggs.77.89;
RA Goto D.B., Ogi M., Kijima F., Kumagai T., van Werven F., Onouchi H.,
RA Naito S.;
RT "A single-nucleotide mutation in a gene encoding S-adenosylmethionine
RT synthetase is associated with methionine over-accumulation phenotype in
RT Arabidopsis thaliana.";
RL Genes Genet. Syst. 77:89-95(2002).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ALA-120.
RX PubMed=11844113; DOI=10.1046/j.1365-313x.2002.01221.x;
RA Shen B., Li C., Tarczynski M.C.;
RT "High free-methionine and decreased lignin content result from a mutation
RT in the Arabidopsis S-adenosyl-L-methionine synthetase 3 gene.";
RL Plant J. 29:371-380(2002).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR.
RX PubMed=16365035; DOI=10.1074/jbc.m511635200;
RA Lindermayr C., Saalbach G., Bahnweg G., Durner J.;
RT "Differential inhibition of Arabidopsis methionine adenosyltransferases by
RT protein S-nitrosylation.";
RL J. Biol. Chem. 281:4285-4291(2006).
RN [7]
RP INTERACTION WITH GRF3.
RX PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
RA Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
RT "14-3-3 proteins fine-tune plant nutrient metabolism.";
RL FEBS Lett. 585:143-147(2011).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. The reaction comprises two steps that are both
CC catalyzed by the same enzyme: formation of S-adenosylmethionine
CC (AdoMet) and triphosphate, and subsequent hydrolysis of the
CC triphosphate (PubMed:12087191, PubMed:16365035). Involved in the
CC biosynthesis of lignin (PubMed:11844113). {ECO:0000269|PubMed:11844113,
CC ECO:0000269|PubMed:12087191, ECO:0000269|PubMed:16365035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC Evidence={ECO:0000269|PubMed:16365035};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16365035};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Note=Binds 2 divalent ions per subunit. The metal ions interact
CC primarily with the substrate (By similarity). Can utilize magnesium,
CC manganese or cobalt (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P13444, ECO:0000250|UniProtKB:Q96551};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000305|PubMed:16365035};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate (By similarity).
CC {ECO:0000250|UniProtKB:P13444};
CC -!- ACTIVITY REGULATION: Inhibited by 5,5'-dithiobis-2-nitrobenzoic acid
CC (DTNB) and N-ethylmaleimide (NEM) (in vitro).
CC {ECO:0000269|PubMed:16365035}.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000269|PubMed:12087191, ECO:0000269|PubMed:16365035}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with GRF3.
CC {ECO:0000250|UniProtKB:Q00266, ECO:0000269|PubMed:21094157}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; AC006922; AAD31573.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09310.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09311.1; -; Genomic_DNA.
DR EMBL; AF367310; AAK32897.1; -; mRNA.
DR EMBL; AY133601; AAM91431.1; -; mRNA.
DR PIR; G84785; G84785.
DR RefSeq; NP_001118458.1; NM_001124986.1.
DR RefSeq; NP_181225.1; NM_129243.4.
DR AlphaFoldDB; Q9SJL8; -.
DR SMR; Q9SJL8; -.
DR BioGRID; 3604; 7.
DR STRING; 3702.AT2G36880.2; -.
DR MetOSite; Q9SJL8; -.
DR PaxDb; Q9SJL8; -.
DR PRIDE; Q9SJL8; -.
DR ProteomicsDB; 232238; -.
DR EnsemblPlants; AT2G36880.1; AT2G36880.1; AT2G36880.
DR EnsemblPlants; AT2G36880.2; AT2G36880.2; AT2G36880.
DR GeneID; 818260; -.
DR Gramene; AT2G36880.1; AT2G36880.1; AT2G36880.
DR Gramene; AT2G36880.2; AT2G36880.2; AT2G36880.
DR KEGG; ath:AT2G36880; -.
DR Araport; AT2G36880; -.
DR TAIR; locus:2058011; AT2G36880.
DR eggNOG; KOG1506; Eukaryota.
DR HOGENOM; CLU_041802_0_1_1; -.
DR InParanoid; Q9SJL8; -.
DR OMA; KEFPWEQ; -.
DR OrthoDB; 685006at2759; -.
DR PhylomeDB; Q9SJL8; -.
DR BioCyc; ARA:AT2G36880-MON; -.
DR BRENDA; 2.5.1.6; 399.
DR UniPathway; UPA00315; UER00080.
DR PRO; PR:Q9SJL8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJL8; baseline and differential.
DR Genevisible; Q9SJL8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IMP:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00086; S_AdoMet_synth1; 1.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cobalt; Cytoplasm; Lignin biosynthesis; Magnesium;
KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium;
KW Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="S-adenosylmethionine synthase 3"
FT /id="PRO_0000363003"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 43
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 56
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 99
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 167..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 235..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 246
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 252..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 277
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT MUTAGEN 120
FT /note="A->T: In mto3-1; accumulation of free Met, increased
FT resistance to Ethionine, and reduced lignin formation."
FT /evidence="ECO:0000269|PubMed:11844113"
FT MUTAGEN 167
FT /note="D->N: In mto3-2; accumulation of free Met and
FT increased resistance to Ethionine."
FT /evidence="ECO:0000269|PubMed:12087191"
SQ SEQUENCE 390 AA; 42497 MW; 5C8BB48838606184 CRC64;
METFLFTSES VNEGHPDKLC DQISDAILDA CLEQDPESKV ACETCTKTNM VMVFGEITTA
AKVDYEKIVR STCREIGFIS ADVGLDADKC NVLVNIEQQS PDIAQGVHGH LTKKPEDIGA
GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNKT CPWLRPDGKT QVTVEYKNDG
GAMIPIRVHT VLISTQHDET VTNDEIAADL KEHVIKPVIP AKYLDDNTIF HLNPSGRFVI
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVAAGLAR
RCIVQVSYAI GVPEPLSVFV DTYKTGTIPD KDILVLIKEA FDFRPGMMAI NLDLKRGGNF
RFQKTAAYGH FGRDDPDFTW EVVKPLKPKA
