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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publications

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.UniRule 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

  1. KM=3.0 mM for Mg2+1 Publication
  2. KM=0.11 mM for ATP1 Publication
  3. KM=0.08 mM for L-methionine1 Publication

    Pathwayi: S-adenosyl-L-methionine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.UniRule annotation6 Publications
    Proteins known to be involved in this subpathway in this organism are:
    1. S-adenosylmethionine synthase (metK)
    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 keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei15ATPUniRule annotationCombined sources1 Publication1
    Metal bindingi17MagnesiumUniRule annotationCombined sources1 Publication1
    Metal bindingi43PotassiumUniRule annotationCombined sources1 Publication1 Publication1
    Binding sitei56MethionineUniRule annotationCombined sources1 Publication1
    Binding sitei99MethionineUniRule annotationCombined sources1 Publication1
    Binding sitei239ATP; shared with neighboring subunitUniRule annotationCombined sources1 Publication1
    Binding sitei239Methionine; shared with neighboring subunitUniRule annotationCombined sources1 Publication1
    Binding sitei262ATP; via amide nitrogen; shared with neighboring subunitUniRule annotationCombined sources1 Publication1
    Binding sitei266ATP; shared with neighboring subunitUniRule annotationCombined sources1 Publication1
    Binding sitei270MethionineUniRule annotationCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi164 – 166ATPUniRule annotationCombined sources1 Publication3
    Nucleotide bindingi230 – 231ATPUniRule annotationCombined sources1 Publication2
    Nucleotide bindingi245 – 246ATPUniRule annotationCombined sources1 Publication2

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • magnesium ion binding Source: EcoCyc
    • methionine adenosyltransferase activity Source: EcoCyc
    • potassium ion binding Source: EcoCyc

    GO - Biological processi

    • one-carbon metabolic process Source: UniProtKB-HAMAP
    • S-adenosylmethionine biosynthetic process Source: EcoCyc
    • S-adenosylmethionine cycle Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Cobalt, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Potassium

    Enzyme and pathway databases

    BioCyciEcoCyc:S-ADENMETSYN-MONOMER.
    ECOL316407:JW2909-MONOMER.
    MetaCyc:S-ADENMETSYN-MONOMER.
    BRENDAi2.5.1.6. 2026.
    SABIO-RKP0A817.
    UniPathwayiUPA00315; 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
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10589. metK.

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells are resistant to methionine-analogs, such as DL-ethionine(Et).1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi15H → N: Loss of activity. 1 Publication1
    Mutagenesisi17D → N or A: Loss of activity. 1 Publication1
    Mutagenesisi43E → K: Misfolding and subject to proteolytic degradation. 1 Publication1
    Mutagenesisi43E → Q: Nearly abolishes enzyme activity. Abolishes stimulation of enzyme activity by potassium. 1 Publication1
    Mutagenesisi90C → A or S: Decrease in the homotetramer formation capability. Enhanced thermal stability. 1 Publication1
    Mutagenesisi119D → N: Decrease of both AdoMet synthesis and AdoMet-activated tripolyphosphate hydrolysis. 1 Publication1
    Mutagenesisi166K → M: Decrease in AdoMet synthesis. 1 Publication1
    Mutagenesisi239D → N: Decrease in AdoMet synthesis. 1 Publication1
    Mutagenesisi240C → A: Decrease in AdoMet synthesis. 1 Publication1
    Mutagenesisi245R → H or L: Loss of activity. 1 Publication1
    Mutagenesisi246K → M: Loss of activity. Modification in protein conformation. 1 Publication1
    Mutagenesisi266K → A: Loss of activity. 1 Publication1
    Mutagenesisi266K → M: Unstable; trace activity. 1 Publication1
    Mutagenesisi270K → M: Decrease in activity. 1 Publication1
    Mutagenesisi272D → N or A: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00001745182 – 384S-adenosylmethionine synthaseAdd BLAST383

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei3N6-acetyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP0A817.
    PaxDbiP0A817.
    PRIDEiP0A817.

    2D gel databases

    SWISS-2DPAGEP0A817.

    Expressioni

    Inductioni

    AdoMet activates the tripolyphosphatase reaction.

    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 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-546295,EBI-546295
    groLP0A6F52EBI-546295,EBI-543750

    Protein-protein interaction databases

    BioGridi4260657. 210 interactors.
    DIPiDIP-35672N.
    IntActiP0A817. 38 interactors.
    MINTiMINT-1233798.
    STRINGi511145.b2942.

    Structurei

    Secondary structure

    1384
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 11Combined sources8
    Helixi16 – 34Combined sources19
    Beta strandi39 – 47Combined sources9
    Beta strandi50 – 58Combined sources9
    Helixi65 – 76Combined sources12
    Helixi81 – 83Combined sources3
    Turni87 – 89Combined sources3
    Beta strandi90 – 97Combined sources8
    Helixi101 – 107Combined sources7
    Turni112 – 114Combined sources3
    Beta strandi117 – 119Combined sources3
    Beta strandi121 – 128Combined sources8
    Helixi137 – 154Combined sources18
    Beta strandi156 – 158Combined sources3
    Beta strandi161 – 174Combined sources14
    Beta strandi177 – 190Combined sources14
    Beta strandi192 – 194Combined sources3
    Helixi196 – 206Combined sources11
    Turni207 – 211Combined sources5
    Helixi214 – 216Combined sources3
    Beta strandi222 – 226Combined sources5
    Helixi235 – 238Combined sources4
    Beta strandi239 – 242Combined sources4
    Turni247 – 254Combined sources8
    Helixi271 – 288Combined sources18
    Beta strandi291 – 301Combined sources11
    Beta strandi309 – 314Combined sources6
    Beta strandi319 – 321Combined sources3
    Helixi323 – 333Combined sources11
    Helixi338 – 345Combined sources8
    Beta strandi348 – 350Combined sources3
    Helixi353 – 356Combined sources4
    Beta strandi360 – 362Combined sources3
    Beta strandi364 – 366Combined sources3
    Turni367 – 369Combined sources3
    Helixi373 – 379Combined sources7
    Turni380 – 382Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FUGX-ray3.20A/B2-384[»]
    1MXAX-ray2.80A2-384[»]
    1MXBX-ray2.80A2-384[»]
    1MXCX-ray3.00A2-384[»]
    1P7LX-ray2.50A/B/C/D2-384[»]
    1RG9X-ray2.50A/B/C/D2-384[»]
    1XRAX-ray3.00A2-384[»]
    1XRBX-ray3.00A2-384[»]
    1XRCX-ray3.00A2-384[»]
    ProteinModelPortaliP0A817.
    SMRiP0A817.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A817.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni99 – 109Flexible loopUniRule annotation1 PublicationAdd BLAST11

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CPH. Bacteria.
    COG0192. LUCA.
    HOGENOMiHOG000245710.
    InParanoidiP0A817.
    KOiK00789.
    OMAiDNFLAFD.
    PhylomeDBiP0A817.

    Family and domain databases

    HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
    InterProiIPR022631. 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.
    [Graphical view]
    PANTHERiPTHR11964. PTHR11964. 1 hit.
    PfamiPF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000497. MAT. 1 hit.
    SUPFAMiSSF55973. SSF55973. 3 hits.
    TIGRFAMsiTIGR01034. metK. 1 hit.
    PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A817-1 [UniParc]FASTAAdd to basket

    « Hide

            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
    Length:384
    Mass (Da):41,952
    Last modified:January 23, 2007 - v2
    Checksum:i97FA8CF17B542941
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti50 – 61MVLVG…ITTSA → IGFSWRRNHHQRP (PubMed:6094561).CuratedAdd BLAST12
    Sequence conflicti50 – 61MVLVG…ITTSA → IGFSWRRNHHQRP (PubMed:2198270).CuratedAdd BLAST12
    Sequence conflicti123 – 133MFGYATNETDV → DVSATQLMKPTC in AAA24164 (PubMed:6094561).CuratedAdd BLAST11
    Sequence conflicti159 – 161PWL → RV (PubMed:6094561).Curated3
    Sequence conflicti159 – 161PWL → RV (PubMed:8231813).Curated3
    Sequence conflicti172Q → S in AAA24164 (PubMed:6094561).Curated1
    Sequence conflicti252Y → T in AAA24164 (PubMed:6094561).Curated1
    Sequence conflicti305V → L in AAA24164 (PubMed:6094561).Curated1
    Sequence conflicti337Missing (PubMed:6094561).Curated1
    Sequence conflicti339Y → I (PubMed:6094561).Curated1
    Sequence conflicti375 – 376QL → HV (PubMed:8231813).Curated2
    Sequence conflicti378R → P (PubMed:8231813).Curated1

    Mass spectrometryi

    Molecular mass is 41843±10.5 Da from positions 2 - 384. Determined by ESI. 1 Publication

    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.
    PIRiE65079. SYECSM.
    RefSeqiNP_417417.1. NC_000913.3.
    WP_001062128.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75979; AAC75979; b2942.
    BAE77005; BAE77005; BAE77005.
    GeneIDi945389.
    KEGGiecj:JW2909.
    eco:b2942.
    PATRICi32121294. VBIEscCol129921_3035.

    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.
    PIRiE65079. SYECSM.
    RefSeqiNP_417417.1. NC_000913.3.
    WP_001062128.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FUGX-ray3.20A/B2-384[»]
    1MXAX-ray2.80A2-384[»]
    1MXBX-ray2.80A2-384[»]
    1MXCX-ray3.00A2-384[»]
    1P7LX-ray2.50A/B/C/D2-384[»]
    1RG9X-ray2.50A/B/C/D2-384[»]
    1XRAX-ray3.00A2-384[»]
    1XRBX-ray3.00A2-384[»]
    1XRCX-ray3.00A2-384[»]
    ProteinModelPortaliP0A817.
    SMRiP0A817.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260657. 210 interactors.
    DIPiDIP-35672N.
    IntActiP0A817. 38 interactors.
    MINTiMINT-1233798.
    STRINGi511145.b2942.

    2D gel databases

    SWISS-2DPAGEP0A817.

    Proteomic databases

    EPDiP0A817.
    PaxDbiP0A817.
    PRIDEiP0A817.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75979; AAC75979; b2942.
    BAE77005; BAE77005; BAE77005.
    GeneIDi945389.
    KEGGiecj:JW2909.
    eco:b2942.
    PATRICi32121294. VBIEscCol129921_3035.

    Organism-specific databases

    EchoBASEiEB0584.
    EcoGeneiEG10589. metK.

    Phylogenomic databases

    eggNOGiENOG4105CPH. Bacteria.
    COG0192. LUCA.
    HOGENOMiHOG000245710.
    InParanoidiP0A817.
    KOiK00789.
    OMAiDNFLAFD.
    PhylomeDBiP0A817.

    Enzyme and pathway databases

    UniPathwayiUPA00315; UER00080.
    BioCyciEcoCyc:S-ADENMETSYN-MONOMER.
    ECOL316407:JW2909-MONOMER.
    MetaCyc:S-ADENMETSYN-MONOMER.
    BRENDAi2.5.1.6. 2026.
    SABIO-RKP0A817.

    Miscellaneous databases

    EvolutionaryTraceiP0A817.
    PROiP0A817.

    Family and domain databases

    HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
    InterProiIPR022631. 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.
    [Graphical view]
    PANTHERiPTHR11964. PTHR11964. 1 hit.
    PfamiPF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000497. MAT. 1 hit.
    SUPFAMiSSF55973. SSF55973. 3 hits.
    TIGRFAMsiTIGR01034. metK. 1 hit.
    PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMETK_ECOLI
    AccessioniPrimary (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: November 2, 2016
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to differ from MetX, which was assigned as a second AdoMet synthase before being shown to be identical to MetK.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.