ID METK3_PICSI Reviewed; 394 AA. AC A9P2P4; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 56. DE RecName: Full=S-adenosylmethionine synthase 3; DE Short=AdoMet synthase 3; DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551}; DE AltName: Full=Methionine adenosyltransferase 3; DE Short=MAT 3; GN Name=METK3; OS Picea sitchensis (Sitka spruce) (Pinus sitchensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea. OX NCBI_TaxID=3332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. FB3-425; TISSUE=Shoot; RA Ralph S.G., Kirkpatrick R., Chun H.J.E., Palmquist D., Wynhoven B., RA Kolosova N., Cooper N., Oddy C., Jancsik S., Ritland C.E., Douglas C.J., RA Butterfield Y.S.N., Liu J., Stott J., Yang G., Barber S., Holt R.A., RA Siddiqui A., Jones S.J.M., Marra M.A., Ritland K., Bohlmann J.; RT "The spruce transcriptome: analysis of ca. 6,500 sequence-verified full- RT length cDNAs."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. 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=L-methionine + ATP + H2O = S-adenosyl-L-methionine + phosphate CC + diphosphate; 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:0000250}. 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; EF087924; ABK27155.1; -; mRNA. DR AlphaFoldDB; A9P2P4; -. DR SMR; A9P2P4; -. DR UniPathway; UPA00315; UER00080. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004478; F:methionine adenosyltransferase activity; ISS:UniProtKB. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd18079; S-AdoMet_synt; 1. DR FunFam; 3.30.300.10:FF:000001; S-adenosylmethionine synthase; 1. DR FunFam; 3.30.300.10:FF:000003; S-adenosylmethionine synthase; 1. DR FunFam; 3.30.300.10:FF:000004; S-adenosylmethionine synthase; 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; 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; PS00377; ADOMET_SYNTHASE_2; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cobalt; Cytoplasm; Magnesium; Metal-binding; KW Nucleotide-binding; One-carbon metabolism; Potassium; Transferase. FT CHAIN 1..394 FT /note="S-adenosylmethionine synthase 3" FT /id="PRO_0000363039" 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" SQ SEQUENCE 394 AA; 43097 MW; A85E6CD628CA3121 CRC64; METFLFTSES VNEGHPDKLC DQISDAVLDA CLTQDPDSKV ACETCTKTNM VMVFGEITTK ADVDYEQIVR KTCREIGFIS DDVGLDADHC KVLVNIEQQS PDIAQGVHGH FTKRPEEIGA GYQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNGT CAWLRPDGKT QVTIEYRNDG GAMVPERVHT VLISTQHDET VTNDQIAADL KQHVIKPVIP EKYLDENTIF HLNPSGRFVI GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVAAGLAR RCLVQVSYAI GVPEPLSVFV DSYGTGTIPD KVILELIKKN FDFRPGMITI NLDLKRGGNG RFQKTAAYGH FGRDDPDFTW EIVKPLKQEK ALPA //