ID   METK4_ARATH             Reviewed;         393 AA.
AC   Q9LUT2; Q0WLR3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=S-adenosylmethionine synthase 4;
DE            Short=AdoMet synthase 4;
DE            EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551};
DE   AltName: Full=Methionine adenosyltransferase 4;
DE            Short=MAT 4;
GN   Name=METK4; Synonyms=MTO3, SAMS3; OrderedLocusNames=At3g17390;
GN   ORFNames=MGD8.23;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14505352; DOI=10.1002/jcb.10624;
RA   Calikowski T.T., Meulia T., Meier I.;
RT   "A proteomic study of the Arabidopsis nuclear matrix.";
RL   J. Cell. Biochem. 90:361-378(2003).
RN   [7]
RP   TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15276459; DOI=10.1016/j.phytochem.2004.03.026;
RA   Wienkoop S., Zoeller D., Ebert B., Simon-Rosin U., Fisahn J., Glinski M.,
RA   Weckwerth W.;
RT   "Cell-specific protein profiling in Arabidopsis thaliana trichomes:
RT   identification of trichome-located proteins involved in sulfur metabolism
RT   and detoxification.";
RL   Phytochemistry 65:1641-1649(2004).
RN   [8]
RP   INDUCTION BY COLD, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16574749; DOI=10.1093/jxb/erj129;
RA   Amme S., Matros A., Schlesier B., Mock H.-P.;
RT   "Proteome analysis of cold stress response in Arabidopsis thaliana using
RT   DIGE-technology.";
RL   J. Exp. Bot. 57:1537-1546(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
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. {ECO:0000250|UniProtKB:Q96551}.
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:0000250|UniProtKB:Q96551};
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:0000250|UniProtKB:Q96551};
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:0000250|UniProtKB:Q96551};
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   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q96551}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14505352}.
CC   -!- TISSUE SPECIFICITY: Detected in trichomes (at the protein level).
CC       {ECO:0000269|PubMed:15276459}.
CC   -!- INDUCTION: Induced by cold. {ECO:0000269|PubMed:16574749}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB022216; BAB02743.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75948.1; -; Genomic_DNA.
DR   EMBL; AY037214; AAK59799.1; -; mRNA.
DR   EMBL; AY120708; AAM53266.1; -; mRNA.
DR   EMBL; BT000712; AAN31855.1; -; mRNA.
DR   EMBL; BT002665; AAO11581.1; -; mRNA.
DR   EMBL; AK230129; BAF01944.1; -; mRNA.
DR   EMBL; AY087184; AAM64740.1; -; mRNA.
DR   RefSeq; NP_188365.1; NM_112618.4.
DR   AlphaFoldDB; Q9LUT2; -.
DR   SMR; Q9LUT2; -.
DR   BioGRID; 6336; 13.
DR   IntAct; Q9LUT2; 2.
DR   MINT; Q9LUT2; -.
DR   STRING; 3702.Q9LUT2; -.
DR   iPTMnet; Q9LUT2; -.
DR   SwissPalm; Q9LUT2; -.
DR   PaxDb; 3702-AT3G17390-1; -.
DR   ProteomicsDB; 232239; -.
DR   EnsemblPlants; AT3G17390.1; AT3G17390.1; AT3G17390.
DR   GeneID; 821003; -.
DR   Gramene; AT3G17390.1; AT3G17390.1; AT3G17390.
DR   KEGG; ath:AT3G17390; -.
DR   Araport; AT3G17390; -.
DR   TAIR; AT3G17390; MTO3.
DR   eggNOG; KOG1506; Eukaryota.
DR   HOGENOM; CLU_041802_0_1_1; -.
DR   InParanoid; Q9LUT2; -.
DR   OMA; ASYMARY; -.
DR   OrthoDB; 446435at2759; -.
DR   PhylomeDB; Q9LUT2; -.
DR   BioCyc; ARA:AT3G17390-MONOMER; -.
DR   BRENDA; 2.5.1.6; 399.
DR   UniPathway; UPA00315; UER00080.
DR   PRO; PR:Q9LUT2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LUT2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; ISS:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR   GO; GO:0006555; P:methionine metabolic process; IMP:TAIR.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd18079; S-AdoMet_synt; 1.
DR   Gene3D; 3.30.300.10; -; 3.
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   NCBIfam; TIGR01034; metK; 1.
DR   PANTHER; PTHR11964:SF81; S-ADENOSYLMETHIONINE SYNTHASE 4; 1.
DR   PANTHER; PTHR11964; S-ADENOSYLMETHIONINE SYNTHETASE; 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; S-adenosylmethionine synthetase; 3.
DR   PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR   PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
DR   Genevisible; Q9LUT2; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalt; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome;
KW   Transferase.
FT   CHAIN           1..393
FT                   /note="S-adenosylmethionine synthase 4"
FT                   /id="PRO_0000363004"
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   CONFLICT        198
FT                   /note="D -> G (in Ref. 4; BAF01944)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  42796 MW;  70034EC2B5E81867 CRC64;
     MESFLFTSES VNEGHPDKLC DQISDAILDA CLEQDPESKV ACETCTKTNM VMVFGEITTK
     ANVDYEQIVR KTCREIGFVS ADVGLDADNC KVLVNIEQQS PDIAQGVHGH LTKKPEEVGA
     GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNGT CPWLRPDGKT QVTIEYINES
     GAMVPVRVHT VLISTQHDET VTNDEIAADL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI
     GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVASGLAR
     RVIVQVSYAI GVPEPLSVFV DSYGTGKIPD KEILEIVKES FDFRPGMISI NLDLKRGGNG
     RFLKTAAYGH FGRDDADFTW EVVKPLKSNK VQA
//