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UniProt functional annotation for P0A817 | ||
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| UniProt code: P0A817. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the formation of S-adenosylmethionine (AdoMet) 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 (PubMed:6251075, PubMed:7629147, PubMed:7629176, PubMed:9753435, PubMed:10551856, PubMed:10660564). Is essential for growth (PubMed:11952912). {ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:11952912, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435}. |
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| Catalytic activity: | |
Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S- adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:6251075}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:6251075}; Note=Binds 2 divalent ions per subunit. The ions interact primarily with the substrate. {ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562, ECO:0000305|PubMed:10551856, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9}; |
| Cofactor: | |
Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562}; Note=Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate. {ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=3.0 mM for Mg(2+) {ECO:0000269|PubMed:7629147}; KM=0.11 mM for ATP {ECO:0000269|PubMed:7629147}; KM=0.08 mM for L-methionine {ECO:0000269|PubMed:7629147}; |
| Pathway: | |
Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435}. |
| Subunit: | |
Homotetramer; dimer of dimers (PubMed:6251075, PubMed:7629147, PubMed:7629176, PubMed:10660564, PubMed:8550549, PubMed:8611562, PubMed:8723769, PubMed:14967023). The active sites are at the interface between subunits; each dimer has two active sites (PubMed:8550549, PubMed:8611562, PubMed:8723769, PubMed:14967023). {ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:14967023, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:8550549, ECO:0000269|PubMed:8611562, ECO:0000269|PubMed:8723769}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}. |
| Induction: | |
AdoMet activates the tripolyphosphatase reaction. |
| Mass spectrometry: | |
Mass=41843; Mass_error=10.5; Method=Electrospray; Evidence={ECO:0000269|PubMed:8550549}; |
| Disruption phenotype: | |
Cells are resistant to methionine-analogs, such as DL-ethionine(Et). {ECO:0000269|PubMed:8231813}. |
| Similarity: | |
Belongs to the AdoMet synthase family. {ECO:0000255|HAMAP- Rule:MF_00086}. |
Annotations taken from UniProtKB at the EBI.