UniProtKB - P0A817 (METK_ECOLI)
S-adenosylmethionine synthase
metK
Functioni
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).
7 PublicationsCaution
Catalytic activityi
- ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionineUniRule annotation6 PublicationsEC:2.5.1.6UniRule annotation6 Publications
Cofactori
Protein has several cofactor binding sites:- Mg2+UniRule annotation5 Publications, Mn2+1 Publication, Co2+1 PublicationNote: Binds 2 divalent ions per subunit. The ions interact primarily with the substrate.Combined sources1 Publication3 Publications
- K+UniRule annotation5 PublicationsNote: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.Combined sources4 Publications
Kineticsi
- KM=3.0 mM for Mg2+1 Publication
- KM=0.11 mM for ATP1 Publication
- KM=0.08 mM for L-methionine1 Publication
: S-adenosyl-L-methionine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.UniRule annotation6 Publications This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 15 | ATPUniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 17 | MagnesiumUniRule annotationCombined sources1 Publication | 1 | |
Metal bindingi | 43 | PotassiumUniRule annotationCombined sources1 Publication1 Publication | 1 | |
Binding sitei | 56 | MethionineUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 99 | MethionineUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 239 | ATP; shared with neighboring subunitUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 239 | Methionine; shared with neighboring subunitUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 262 | ATP; via amide nitrogen; shared with neighboring subunitUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 266 | ATP; shared with neighboring subunitUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 270 | MethionineUniRule annotationCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 164 – 166 | ATPUniRule annotationCombined sources1 Publication | 3 | |
Nucleotide bindingi | 230 – 231 | ATPUniRule annotationCombined sources1 Publication | 2 | |
Nucleotide bindingi | 245 – 246 | ATPUniRule annotationCombined sources1 Publication | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- identical protein binding Source: IntAct
- magnesium ion binding Source: EcoCyc
- methionine adenosyltransferase activity Source: EcoCyc
- potassium ion binding Source: EcoCyc
GO - Biological processi
- one-carbon metabolic process Source: UniProtKB-UniRule
- S-adenosylmethionine biosynthetic process Source: EcoCyc
- S-adenosylmethionine cycle Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | One-carbon metabolism |
Ligand | ATP-binding, Cobalt, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Potassium |
Enzyme and pathway databases
BioCyci | EcoCyc:S-ADENMETSYN-MONOMER |
BRENDAi | 2.5.1.6, 2026 |
SABIO-RKi | P0A817 |
UniPathwayi | UPA00315;UER00080 |
Names & Taxonomyi
Protein namesi | Recommended name: S-adenosylmethionine synthaseUniRule annotation (EC:2.5.1.6UniRule annotation6 Publications)Short name: AdoMet synthaseUniRule annotation Alternative name(s): MATUniRule annotation Methionine adenosyltransferaseUniRule annotation |
Gene namesi | Name:metKUniRule annotation Synonyms:metX Ordered Locus Names:b2942, JW2909 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 15 | H → N: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 17 | D → N or A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 43 | E → K: Misfolding and subject to proteolytic degradation. 1 Publication | 1 | |
Mutagenesisi | 43 | E → Q: Nearly abolishes enzyme activity. Abolishes stimulation of enzyme activity by potassium. 1 Publication | 1 | |
Mutagenesisi | 90 | C → A or S: Decrease in the homotetramer formation capability. Enhanced thermal stability. 1 Publication | 1 | |
Mutagenesisi | 119 | D → N: Decrease of both AdoMet synthesis and AdoMet-activated tripolyphosphate hydrolysis. 1 Publication | 1 | |
Mutagenesisi | 166 | K → M: Decrease in AdoMet synthesis. 1 Publication | 1 | |
Mutagenesisi | 239 | D → N: Decrease in AdoMet synthesis. 1 Publication | 1 | |
Mutagenesisi | 240 | C → A: Decrease in AdoMet synthesis. 1 Publication | 1 | |
Mutagenesisi | 245 | R → H or L: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 246 | K → M: Loss of activity. Modification in protein conformation. 1 Publication | 1 | |
Mutagenesisi | 266 | K → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 266 | K → M: Unstable; trace activity. 1 Publication | 1 | |
Mutagenesisi | 270 | K → M: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 272 | D → N or A: Loss of activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000174518 | 2 – 384 | S-adenosylmethionine synthaseAdd BLAST | 383 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A817 |
PaxDbi | P0A817 |
PRIDEi | P0A817 |
2D gel databases
SWISS-2DPAGEi | P0A817 |
PTM databases
iPTMneti | P0A817 |
Expressioni
Inductioni
Interactioni
Subunit structurei
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).
7 PublicationsBinary interactionsi
P0A817
With | #Exp. | IntAct |
---|---|---|
groEL [P0A6F5] | 2 | EBI-546295,EBI-543750 |
itself | 2 | EBI-546295,EBI-546295 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4260657, 257 interactors |
DIPi | DIP-35672N |
IntActi | P0A817, 39 interactors |
MINTi | P0A817 |
STRINGi | 511145.b2942 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P0A817 |
SMRi | P0A817 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A817 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 99 – 109 | Flexible loopUniRule annotation1 PublicationAdd BLAST | 11 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0192, Bacteria |
HOGENOMi | CLU_041802_1_1_6 |
InParanoidi | P0A817 |
OMAi | MPYLRPD |
PhylomeDBi | P0A817 |
Family and domain databases
HAMAPi | MF_00086, S_AdoMet_synth1, 1 hit |
InterProi | View protein in InterPro IPR022631, ADOMET_SYNTHASE_CS IPR022630, S-AdoMet_synt_C IPR022629, S-AdoMet_synt_central IPR022628, S-AdoMet_synt_N IPR002133, S-AdoMet_synthetase IPR022636, S-AdoMet_synthetase_sfam |
PANTHERi | PTHR11964, PTHR11964, 1 hit |
Pfami | View protein in Pfam PF02773, S-AdoMet_synt_C, 1 hit PF02772, S-AdoMet_synt_M, 1 hit PF00438, S-AdoMet_synt_N, 1 hit |
PIRSFi | PIRSF000497, MAT, 1 hit |
SUPFAMi | SSF55973, SSF55973, 3 hits |
TIGRFAMsi | TIGR01034, metK, 1 hit |
PROSITEi | View protein in PROSITE PS00376, ADOMET_SYNTHASE_1, 1 hit PS00377, ADOMET_SYNTHASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM
60 70 80 90 100
VLVGGEITTS AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS
110 120 130 140 150
PDINQGVDRA DPLEQGAGDQ GLMFGYATNE TDVLMPAPIT YAHRLVQRQA
160 170 180 190 200
EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG IDAVVLSTQH SEEIDQKSLQ
210 220 230 240 250
EAVMEEIIKP ILPAEWLTSA TKFFINPTGR FVIGGPMGDC GLTGRKIIVD
260 270 280 290 300
TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS
310 320 330 340 350
YAIGVAEPTS IMVETFGTEK VPSEQLTLLV REFFDLRPYG LIQMLDLLHP
360 370 380
IYKETAAYGH FGREHFPWEK TDKAQLLRDA AGLK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 50 – 61 | MVLVG…ITTSA → IGFSWRRNHHQRP (PubMed:6094561).CuratedAdd BLAST | 12 | |
Sequence conflicti | 50 – 61 | MVLVG…ITTSA → IGFSWRRNHHQRP (PubMed:2198270).CuratedAdd BLAST | 12 | |
Sequence conflicti | 123 – 133 | MFGYATNETDV → DVSATQLMKPTC in AAA24164 (PubMed:6094561).CuratedAdd BLAST | 11 | |
Sequence conflicti | 159 – 161 | PWL → RV (PubMed:6094561).Curated | 3 | |
Sequence conflicti | 159 – 161 | PWL → RV (PubMed:8231813).Curated | 3 | |
Sequence conflicti | 172 | Q → S in AAA24164 (PubMed:6094561).Curated | 1 | |
Sequence conflicti | 252 | Y → T in AAA24164 (PubMed:6094561).Curated | 1 | |
Sequence conflicti | 305 | V → L in AAA24164 (PubMed:6094561).Curated | 1 | |
Sequence conflicti | 337 | Missing (PubMed:6094561).Curated | 1 | |
Sequence conflicti | 339 | Y → I (PubMed:6094561).Curated | 1 | |
Sequence conflicti | 375 – 376 | QL → HV (PubMed:8231813).Curated | 2 | |
Sequence conflicti | 378 | R → P (PubMed:8231813).Curated | 1 |
Mass spectrometryi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02129 Genomic DNA Translation: AAA24164.1 U28377 Genomic DNA Translation: AAA69109.1 U00096 Genomic DNA Translation: AAC75979.1 AP009048 Genomic DNA Translation: BAE77005.1 M98266 Genomic DNA Translation: AAB05197.1 M31770 Genomic DNA Translation: AAA24645.2 |
PIRi | E65079, SYECSM |
RefSeqi | NP_417417.1, NC_000913.3 WP_001062128.1, NZ_STEB01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC75979; AAC75979; b2942 BAE77005; BAE77005; BAE77005 |
GeneIDi | 66673177 945389 |
KEGGi | ecj:JW2909 eco:b2942 |
PATRICi | fig|1411691.4.peg.3791 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02129 Genomic DNA Translation: AAA24164.1 U28377 Genomic DNA Translation: AAA69109.1 U00096 Genomic DNA Translation: AAC75979.1 AP009048 Genomic DNA Translation: BAE77005.1 M98266 Genomic DNA Translation: AAB05197.1 M31770 Genomic DNA Translation: AAA24645.2 |
PIRi | E65079, SYECSM |
RefSeqi | NP_417417.1, NC_000913.3 WP_001062128.1, NZ_STEB01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FUG | X-ray | 3.20 | A/B | 2-384 | [»] | |
1MXA | X-ray | 2.80 | A | 2-384 | [»] | |
1MXB | X-ray | 2.80 | A | 2-384 | [»] | |
1MXC | X-ray | 3.00 | A | 2-384 | [»] | |
1P7L | X-ray | 2.50 | A/B/C/D | 2-384 | [»] | |
1RG9 | X-ray | 2.50 | A/B/C/D | 2-384 | [»] | |
1XRA | X-ray | 3.00 | A | 2-384 | [»] | |
1XRB | X-ray | 3.00 | A | 2-384 | [»] | |
1XRC | X-ray | 3.00 | A | 2-384 | [»] | |
7OCK | electron microscopy | 3.60 | B/C/D/E/F/G/H/I | 1-384 | [»] | |
AlphaFoldDBi | P0A817 | |||||
SMRi | P0A817 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260657, 257 interactors |
DIPi | DIP-35672N |
IntActi | P0A817, 39 interactors |
MINTi | P0A817 |
STRINGi | 511145.b2942 |
PTM databases
iPTMneti | P0A817 |
2D gel databases
SWISS-2DPAGEi | P0A817 |
Proteomic databases
jPOSTi | P0A817 |
PaxDbi | P0A817 |
PRIDEi | P0A817 |
Genome annotation databases
EnsemblBacteriai | AAC75979; AAC75979; b2942 BAE77005; BAE77005; BAE77005 |
GeneIDi | 66673177 945389 |
KEGGi | ecj:JW2909 eco:b2942 |
PATRICi | fig|1411691.4.peg.3791 |
Organism-specific databases
EchoBASEi | EB0584 |
Phylogenomic databases
eggNOGi | COG0192, Bacteria |
HOGENOMi | CLU_041802_1_1_6 |
InParanoidi | P0A817 |
OMAi | MPYLRPD |
PhylomeDBi | P0A817 |
Enzyme and pathway databases
UniPathwayi | UPA00315;UER00080 |
BioCyci | EcoCyc:S-ADENMETSYN-MONOMER |
BRENDAi | 2.5.1.6, 2026 |
SABIO-RKi | P0A817 |
Miscellaneous databases
EvolutionaryTracei | P0A817 |
PROi | PR:P0A817 |
Family and domain databases
HAMAPi | MF_00086, S_AdoMet_synth1, 1 hit |
InterProi | View protein in InterPro IPR022631, ADOMET_SYNTHASE_CS IPR022630, S-AdoMet_synt_C IPR022629, S-AdoMet_synt_central IPR022628, S-AdoMet_synt_N IPR002133, S-AdoMet_synthetase IPR022636, S-AdoMet_synthetase_sfam |
PANTHERi | PTHR11964, PTHR11964, 1 hit |
Pfami | View protein in Pfam PF02773, S-AdoMet_synt_C, 1 hit PF02772, S-AdoMet_synt_M, 1 hit PF00438, S-AdoMet_synt_N, 1 hit |
PIRSFi | PIRSF000497, MAT, 1 hit |
SUPFAMi | SSF55973, SSF55973, 3 hits |
TIGRFAMsi | TIGR01034, metK, 1 hit |
PROSITEi | View protein in PROSITE PS00376, ADOMET_SYNTHASE_1, 1 hit PS00377, ADOMET_SYNTHASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | METK_ECOLI | |
Accessioni | P0A817Primary (citable) accession number: P0A817 Secondary accession number(s): P04384, P30869, Q2M9Q1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 20, 1987 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 146 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families