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 02-NOV-2016, entry version 122. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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., RA Hayashizaki Y., 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., RA Glinski M., Weckwerth W.; RT "Cell-specific protein profiling in Arabidopsis thaliana trichomes: RT identification of trichome-located proteins involved in sulfur RT metabolism 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 RT using 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 RT of 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: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC {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 CC magnesium, 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 CC interacts primarily with the substrate (By similarity). CC {ECO:0000250|UniProtKB:P13444}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; 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: Trichomes. {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_112618.3. DR UniGene; At.5781; -. DR UniGene; At.70071; -. DR ProteinModelPortal; Q9LUT2; -. DR SMR; Q9LUT2; -. DR BioGrid; 6336; 8. DR IntAct; Q9LUT2; 2. DR MINT; MINT-8064905; -. DR STRING; 3702.AT3G17390.1; -. DR iPTMnet; Q9LUT2; -. DR SwissPalm; Q9LUT2; -. DR PaxDb; Q9LUT2; -. DR PRIDE; Q9LUT2; -. DR EnsemblPlants; AT3G17390.1; AT3G17390.1; AT3G17390. DR GeneID; 821003; -. DR Gramene; AT3G17390.1; AT3G17390.1; AT3G17390. DR KEGG; ath:AT3G17390; -. DR TAIR; AT3G17390; -. DR eggNOG; KOG1506; Eukaryota. DR eggNOG; COG0192; LUCA. DR HOGENOM; HOG000245710; -. DR InParanoid; Q9LUT2; -. DR KO; K00789; -. DR OMA; SVQHDEC; -. DR OrthoDB; EOG09360BP4; -. DR PhylomeDB; Q9LUT2; -. DR BioCyc; ARA:AT3G17390-MONOMER; -. DR Reactome; R-ATH-156581; Methylation. DR Reactome; R-ATH-1614635; Sulfur amino acid metabolism. DR Reactome; R-ATH-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se. DR UniPathway; UPA00315; UER00080. DR PRO; PR:Q9LUT2; -. DR Proteomes; UP000006548; Chromosome 3. DR Genevisible; Q9LUT2; AT. DR GO; GO:0005618; C:cell wall; IDA:TAIR. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IDA:TAIR. DR GO; GO:0005730; C:nucleolus; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0009506; C:plasmodesma; IDA: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: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 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; Complete proteome; Cytoplasm; Magnesium; KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; KW Reference proteome; Transferase. FT CHAIN 1 393 S-adenosylmethionine synthase 4. FT /FTId=PRO_0000363004. FT NP_BIND 167 169 ATP. {ECO:0000250|UniProtKB:Q00266}. FT NP_BIND 235 238 ATP. {ECO:0000250|UniProtKB:Q00266}. FT NP_BIND 252 253 ATP. {ECO:0000250|UniProtKB:P0A817}. FT METAL 9 9 Magnesium. FT {ECO:0000250|UniProtKB:P13444}. FT METAL 43 43 Potassium. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 15 15 ATP. {ECO:0000250|UniProtKB:Q00266}. FT BINDING 56 56 Methionine. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 99 99 Methionine. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 246 246 ATP. {ECO:0000250|UniProtKB:Q00266}. FT BINDING 246 246 Methionine; shared with neighboring FT subunit. {ECO:0000250|UniProtKB:P0A817}. FT BINDING 269 269 ATP; via amide nitrogen; shared with FT neighboring subunit. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 273 273 ATP; shared with neighboring subunit. FT {ECO:0000250|UniProtKB:P0A817}. FT BINDING 277 277 ATP; shared with neighboring subunit. FT {ECO:0000250|UniProtKB:P13444}. FT BINDING 277 277 Methionine. FT {ECO:0000250|UniProtKB:P0A817}. FT CONFLICT 198 198 D -> G (in Ref. 4; BAF01944). FT {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 //