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
TTAAACAACTGGTAAATATTTTATTAAACTTTGAACTTTATCTAATTTTTCTCATGGTAG
TTCAGTATGGTAACGACCAAAATGTCCATAAGTTGCAGTTTGTTGATAAATTGGTTTTTG
TAAATCTAATGTTTCAATCATTGCTTGGGGACGAAAATCAAAATTTTCTTTAATTGCCTG
CAAAATAATATCATTTGTTACAAAATTAGTTCCAAATGTTTCAACAAAAATTGAAATTGG
TTCAGCCACACCAATTGCATAAGATAATTGAATCTCACATCGTTCAGTTAGTCCTGCTGC
AACAATATTTTTTGCGACATAACGCGCCATATATGCTGCTGAACGATCAACTTTTGTTCC
ATCTTTCCCCGAAAAAGCACCACCACCATGACGAGCATATCCACCATATGTATCAACAAT
AATTTTTCGTCCTGTTAATCCAGCATCACCTTTTGGCCCACCAATTACAAATCGACCAGT
TGGATTAATTAAAACTTTAAAATCTAAATTCATTTTAAATTCTTGCACAACTGGTTCCAT
AATTTCTGTAATAACAAAATGCTTAAATTTAGCTTCATCAATATCTTCATCATGTTGAAT
TGACATTAAGATTGTATCAATATAAATATGTTTAACATTAGTTAAATCTAATGTTACTTG
TGATTTCATATCTGGTCGTGCCCCAATAAACATTCCTTTTTTGCGTAGCATACTTGCTCT
CTTTACTAAGGCATGAGCAATTGAAATTGCTAACGGCATATAATTATCTGATTCATTTGT
TGCATAACCAAACATAATTCCTTGATCACCAGCTCCGGCTTTATCAACACCAATAGAAAT
ATCTGGTGATTGTGTTTTAACTAGTATTTCAACTTCACAATTTTGTCAATCAATTCCTCA
TTCTGCATTATTATACCCAATTTCTTTTAACACTTTCCGTGCTACATTGGCATAATCAAC
CTTTGCTTTTGTCGTAATTTCACCACCAATAATAACCCGATTAGTTGTAATAAAACATTC
ACATGCCACTCGTGATAAGGGGTCTTCTTTTAAACATGCATCTAAAACAGCATCTGAAAT
TTGATCACAAATCTTATCCGGATGTCCTTCTGATACTGATTCTGATGTAAATAAAATTCG
TTCTTTTCCCAT


>protein sequence
MGKERILFTSESVSEGHPDKICDQISDAVLDACLKEDPLSRVACECFITTNRVIIGGEIT
TKAKVDYANVARKVLKEIGYNNAEWGIDWQNCEVEILVKTQSPDISIGVDKAGAGDQGIM
FGYATNESDNYMPLAISIAHALVKRASMLRKKGMFIGARPDMKSQVTLDLTNVKHIYIDT
ILMSIQHDEDIDEAKFKHFVITEIMEPVVQEFKMNLDFKVLINPTGRFVIGGPKGDAGLT
GRKIIVDTYGGYARHGGGAFSGKDGTKVDRSAAYMARYVAKNIVAAGLTERCEIQLSYAI
GVAEPISIFVETFGTNFVTNDIILQAIKENFDFRPQAMIETLDLQKPIYQQTATYGHFGR
YHTELPWEKLDKVQSLIKYLPVV






















© Fisunov Lab of Proteomics, 2016.