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 05-APR-2011, entry version 76. DE RecName: Full=S-adenosylmethionine synthase 4; DE Short=AdoMet synthase 4; DE EC=2.5.1.6; 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; core eudicotyledons; 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 MEDLINE=20277480; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; 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 [3] 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 [4] 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 [5] RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX MEDLINE=22867053; 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 [6] 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 [7] 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 [8] RP UBIQUITINATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=19292762; DOI=10.1111/j.1365-313X.2009.03862.x; RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., RA Vierstra R.D.; RT "Tandem affinity purification and mass spectrometric analysis of RT ubiquitylated proteins in Arabidopsis."; RL Plant J. 59:344-358(2009). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. The overall synthetic reaction is composed of CC two sequential steps, AdoMet formation and the subsequent CC tripolyphosphate hydrolysis which occurs prior to release of CC AdoMet from the enzyme (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt CC (By similarity). CC -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Trichomes. CC -!- INDUCTION: Induced by cold. CC -!- PTM: Ubiquitinated. CC -!- SIMILARITY: Belongs to the AdoMet synthase family. 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; 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 IPI; IPI00536966; -. DR RefSeq; NP_188365.1; NM_112618.3. DR UniGene; At.5781; -. DR UniGene; At.70071; -. DR HSSP; P13444; 1QM4. DR ProteinModelPortal; Q9LUT2; -. DR SMR; Q9LUT2; 3-387. DR STRING; Q9LUT2; -. DR PRIDE; Q9LUT2; -. DR EnsemblPlants; AT3G17390.1; AT3G17390.1; AT3G17390. DR GeneID; 821003; -. DR GenomeReviews; BA000014_GR; AT3G17390. DR KEGG; ath:AT3G17390; -. DR NMPDR; fig|3702.1.peg.13929; -. DR TAIR; At3g17390; -. DR eggNOG; KOG1506; -. DR GeneTree; EPGT00050000019410; -. DR HOGENOM; HBG443662; -. DR InParanoid; Q9LUT2; -. DR OMA; FHDAFIE; -. DR PhylomeDB; Q9LUT2; -. DR ProtClustDB; PLN02243; -. DR ArrayExpress; Q9LUT2; -. DR Genevestigator; Q9LUT2; -. DR GO; GO:0005618; C:cell wall; IDA:TAIR. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; 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; IEA:EC. 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 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; S-AdoMet_synt; 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-AdoMet_synt; 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 Transferase; Ubl conjugation. FT CHAIN 1 393 S-adenosylmethionine synthase 4. FT /FTId=PRO_0000363004. FT NP_BIND 119 124 ATP (Potential). FT NP_BIND 267 274 ATP (Potential). FT METAL 17 17 Magnesium (By similarity). FT METAL 43 43 Potassium (By similarity). FT METAL 271 271 Potassium (By similarity). FT METAL 279 279 Magnesium (By similarity). FT BINDING 147 147 ATP (Potential). FT CONFLICT 198 198 D -> G (in Ref. 3; BAF01944). 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 //