ID A2PZ70_CRYJA Unreviewed; 316 AA. AC A2PZ70; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 58. DE RecName: Full=S-adenosylmethionine synthase {ECO:0000256|RuleBase:RU000541}; DE EC=2.5.1.6 {ECO:0000256|RuleBase:RU000541}; DE Flags: Fragment; GN Name=CC2188 {ECO:0000313|EMBL:BAF46024.1}; OS Cryptomeria japonica (Japanese cedar) (Cupressus japonica). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae; OC Cryptomeria. OX NCBI_TaxID=3369 {ECO:0000313|EMBL:BAF46024.1}; RN [1] {ECO:0000313|EMBL:BAF46024.1} RP NUCLEOTIDE SEQUENCE. RA Kado T., Matsumoto A., Ujino-Ihara T., Tsumura Y.; RT "Amounts and patterns of nucleotide variation within and between two RT Japanese conifers, sugi (Cryptomeria japonica) and hinoki (Chamaecyparis RT obtusa) (Cupressaceae sensu lato)."; RL Tree Genet. Genomes 4:133-141(2008). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. {ECO:0000256|RuleBase:RU000541}. 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:0000256|ARBA:ARBA00001513, CC ECO:0000256|RuleBase:RU000541}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|ARBA:ARBA00001941}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|RuleBase:RU000541}; CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts CC primarily with the substrate. {ECO:0000256|RuleBase:RU000541}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU000541}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU000541}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|RuleBase:RU000541}; CC Note=Binds 2 divalent ions per subunit. The metal ions interact CC primarily with the substrate. Can utilize magnesium, manganese or CC cobalt (in vitro). {ECO:0000256|RuleBase:RU000541}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; CC S-adenosyl-L-methionine from L-methionine: step 1/1. CC {ECO:0000256|ARBA:ARBA00005224, ECO:0000256|RuleBase:RU000541}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the AdoMet synthase family. CC {ECO:0000256|ARBA:ARBA00009685, ECO:0000256|RuleBase:RU004462}. 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; AB264254; BAF46024.1; -; Genomic_DNA. DR AlphaFoldDB; A2PZ70; -. DR UniPathway; UPA00315; UER00080. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:UniProtKB-EC. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. 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 InterPro; IPR022631; ADOMET_SYNTHASE_CS. DR InterPro; IPR022630; S-AdoMet_synt_C. DR InterPro; IPR022629; S-AdoMet_synt_central. DR InterPro; IPR002133; S-AdoMet_synthetase. DR InterPro; IPR022636; S-AdoMet_synthetase_sfam. DR NCBIfam; TIGR01034; metK; 1. DR PANTHER; PTHR11964:SF1; S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-1; 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 SUPFAM; SSF55973; S-adenosylmethionine synthetase; 3. DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000541}; KW Cobalt {ECO:0000256|ARBA:ARBA00023285}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000541}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000541}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000541}; KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, KW ECO:0000256|RuleBase:RU000541}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU000541}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000541}. FT DOMAIN 50..170 FT /note="S-adenosylmethionine synthetase central" FT /evidence="ECO:0000259|Pfam:PF02772" FT DOMAIN 172..313 FT /note="S-adenosylmethionine synthetase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02773" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAF46024.1" FT NON_TER 316 FT /evidence="ECO:0000313|EMBL:BAF46024.1" SQ SEQUENCE 316 AA; 34426 MW; 7D4A34726149791F CRC64; VRKTCREIGF ISDDVGLDAD KCRVLVNIEQ QSPDIAQGVH GHLTKRPEDI GAGDQGHMFG YATDETPELM PLTHVLATKL GAKLTDVRKN GTCPWLRPDG KTQVTIEYKN EKGAMVPLRV HTVLISTQHD ETVTNDQIAA DLKEHVIKPV IPAKYMDENT IFHLNPSGRF VIGGPHGDAG LTGRKIIIDT YGGWGAHGGG AFSGKDPTKV DRSGAYIVRQ AAKSIVAAGL ARRCIVQVSY AIGVPEPLSV FVDSYGTGKI PDKEILNIIK TSFDFRPGMI SINLDLKRGG NGRFQKTAAY GHFGRDDPDF TWEIVK //