SPM_004445
  | Uniprot: A0A037UP85
Description: S-adenosylmethionine synthase EC number: 2.5.1.6 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L-methionine. {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541}. Cofactor: COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541}; ; Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541};; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541}; ; Note=Binds 2 divalent ions per subunit. Magnesium or cobalt. {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541} Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}. Pathway: PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 19 19 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00086}.; METAL 45 45 Potassium. {ECO:0000256|HAMAP-Rule:MF_00086}.; METAL 261 261 Potassium. {ECO:0000256|HAMAP-Rule:MF_00086}.; METAL 269 269 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00086}. Nucleotide binding: NP_BIND 257 264 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}. Site: Gene names (primary): metK Gene names (synonym): Mass: 42,550 Subunit structure [CC]: SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000542}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; methionine adenosyltransferase activity [GO:0004478]; one-carbon metabolic process [GO:0006730]; S-adenosylmethionine biosynthetic process [GO:0006556] Gene ontology IDs: GO:0000287; GO:0004478; GO:0005524; GO:0005737; GO:0006556; GO:0006730 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU004462}. Protein families: AdoMet synthase family Coiled coil: Domain [FT]: DOMAIN 6 103 S-AdoMet_synt_N. {ECO:0000259|Pfam:PF00438}.; DOMAIN 112 228 S-AdoMet_synt_M. {ECO:0000259|Pfam:PF02772}.; DOMAIN 230 369 S-AdoMet_synt_C. {ECO:0000259|Pfam:PF02773}. Motif: Region: EMBL: AGBZ02000003 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92423 UniPathway: CDD: Gene3D: HAMAP: InterPro: MF_00086 PANTHER: IPR022631;IPR022630;IPR022629;IPR022628;IPR002133;IPR022636 PIRSF: PTHR11964 PRINTS: PIRSF000497 PROSITE: Pfam: PS00376;PS00377 ProDom: PF02773;PF02772;PF00438 SMART: SUPFAM: TIGRFAMs: SSF55973 |
50629-51781(-) >nucleotide sequence TTCAGTATGGTAACGACCAAAATGTCCATAAGTTGCAGTTTGTTGATAAATTGGTTTTTG TAAATCTAATGTTTCAATCATTGCTTGGGGACGAAAATCAAAATTTTCTTTAATTGCCTG CAAAATAATATCATTTGTTACAAAATTAGTTCCAAATGTTTCAACAAAAATTGAAATTGG TTCAGCCACACCAATTGCATAAGATAATTGAATCTCACATCGTTCAGTTAGTCCTGCTGC AACAATATTTTTTGCGACATAACGCGCCATATATGCTGCTGAACGATCAACTTTTGTTCC ATCTTTCCCCGAAAAAGCACCACCACCATGACGAGCATATCCACCATATGTATCAACAAT AATTTTTCGTCCTGTTAATCCAGCATCACCTTTTGGCCCACCAATTACAAATCGACCAGT TGGATTAATTAAAACTTTAAAATCTAAATTCATTTTAAATTCTTGCACAACTGGTTCCAT AATTTCTGTAATAACAAAATGCTTAAATTTAGCTTCATCAATATCTTCATCATGTTGAAT TGACATTAAGATTGTATCAATATAAATATGTTTAACATTAGTTAAATCTAATGTTACTTG TGATTTCATATCTGGTCGTGCCCCAATAAACATTCCTTTTTTGCGTAGCATACTTGCTCT CTTTACTAAGGCATGAGCAATTGAAATTGCTAACGGCATATAATTATCTGATTCATTTGT TGCATAACCAAACATAATTCCTTGATCACCAGCTCCGGCTTTATCAACACCAATAGAAAT ATCTGGTGATTGTGTTTTAACTAGTATTTCAACTTCACAATTTTGTCAATCAATTCCTCA TTCTGCATTATTATACCCAATTTCTTTTAACACTTTCCGTGCTACATTGGCATAATCAAC CTTTGCTTTTGTCGTAATTTCACCACCAATAATAACCCGATTAGTTGTAATAAAACATTC ACATGCCACTCGTGATAAGGGGTCTTCTTTTAAACATGCATCTAAAACAGCATCTGAAAT TTGATCACAAATCTTATCCGGATGTCCTTCTGATACTGATTCTGATGTAAATAAAATTCG TTCTTTTCCCAT >protein sequence TKAKVDYANVARKVLKEIGYNNAEWGIDWQNCEVEILVKTQSPDISIGVDKAGAGDQGIM FGYATNESDNYMPLAISIAHALVKRASMLRKKGMFIGARPDMKSQVTLDLTNVKHIYIDT ILMSIQHDEDIDEAKFKHFVITEIMEPVVQEFKMNLDFKVLINPTGRFVIGGPKGDAGLT GRKIIVDTYGGYARHGGGAFSGKDGTKVDRSAAYMARYVAKNIVAAGLTERCEIQLSYAI GVAEPISIFVETFGTNFVTNDIILQAIKENFDFRPQAMIETLDLQKPIYQQTATYGHFGR YHTELPWEKLDKVQSLIKYLPVV |
© Fisunov Lab of Proteomics, 2016.