Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 134 (13 Nov 2019)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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), S-adenosylmethionine synthase (metK), 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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei15ATPUniRule annotationCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi164 – 166ATPUniRule annotationCombined sources1 Publication3
    Nucleotide bindingi230 – 231ATPUniRule annotationCombined sources1 Publication2
    Nucleotide bindingi245 – 246ATPUniRule annotationCombined sources1 Publication2

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionTransferase
    Biological processOne-carbon metabolism
    LigandATP-binding, Cobalt, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Potassium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:S-ADENMETSYN-MONOMER
    ECOL316407:JW2909-MONOMER
    MetaCyc:S-ADENMETSYN-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.5.1.6 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0A817

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00315;UER00080

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:metKUniRule annotation
    Synonyms:metX
    Ordered Locus Names:b2942, JW2909
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001745182 – 384S-adenosylmethionine synthaseAdd BLAST383

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3N6-acetyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0A817

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A817

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0A817

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A817

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0A817

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P0A817

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    AdoMet activates the tripolyphosphatase reaction.

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260657, 257 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-35672N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A817, 39 interactors

    Molecular INTeraction database

    More...
    MINTi
    P0A817

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2942

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1384
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0A817

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0A817

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni99 – 109Flexible loopUniRule annotation1 PublicationAdd BLAST11

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the AdoMet synthase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CPH Bacteria
    COG0192 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000245710

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A817

    KEGG Orthology (KO)

    More...
    KOi
    K00789

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A817

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00086 S_AdoMet_synth1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    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

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11964 PTHR11964, 1 hit

    Pfam protein domain database

    More...
    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

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000497 MAT, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55973 SSF55973, 3 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01034 metK, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00376 ADOMET_SYNTHASE_1, 1 hit
    PS00377 ADOMET_SYNTHASE_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i97FA8CF17B542941
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E65079 SYECSM

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417417.1, NC_000913.3
    WP_001062128.1, NZ_STEB01000001.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75979; AAC75979; b2942
    BAE77005; BAE77005; BAE77005

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945389

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2909
    eco:b2942

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3791

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_STEB01000001.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    SMRiP0A817
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4260657, 257 interactors
    DIPiDIP-35672N
    IntActiP0A817, 39 interactors
    MINTiP0A817
    STRINGi511145.b2942

    PTM databases

    iPTMnetiP0A817

    2D gel databases

    SWISS-2DPAGEiP0A817

    Proteomic databases

    EPDiP0A817
    jPOSTiP0A817
    PaxDbiP0A817
    PRIDEiP0A817

    Genome annotation databases

    EnsemblBacteriaiAAC75979; AAC75979; b2942
    BAE77005; BAE77005; BAE77005
    GeneIDi945389
    KEGGiecj:JW2909
    eco:b2942
    PATRICifig|1411691.4.peg.3791

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0584

    Phylogenomic databases

    eggNOGiENOG4105CPH Bacteria
    COG0192 LUCA
    HOGENOMiHOG000245710
    InParanoidiP0A817
    KOiK00789
    PhylomeDBiP0A817

    Enzyme and pathway databases

    UniPathwayiUPA00315;UER00080
    BioCyciEcoCyc:S-ADENMETSYN-MONOMER
    ECOL316407:JW2909-MONOMER
    MetaCyc:S-ADENMETSYN-MONOMER
    BRENDAi2.5.1.6 2026
    SABIO-RKiP0A817

    Miscellaneous databases

    EvolutionaryTraceiP0A817

    Protein Ontology

    More...
    PROi
    PR:P0A817

    Family and domain databases

    HAMAPiMF_00086 S_AdoMet_synth1, 1 hit
    InterProiView 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
    PANTHERiPTHR11964 PTHR11964, 1 hit
    PfamiView protein in Pfam
    PF02773 S-AdoMet_synt_C, 1 hit
    PF02772 S-AdoMet_synt_M, 1 hit
    PF00438 S-AdoMet_synt_N, 1 hit
    PIRSFiPIRSF000497 MAT, 1 hit
    SUPFAMiSSF55973 SSF55973, 3 hits
    TIGRFAMsiTIGR01034 metK, 1 hit
    PROSITEiView protein in PROSITE
    PS00376 ADOMET_SYNTHASE_1, 1 hit
    PS00377 ADOMET_SYNTHASE_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMETK_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A817
    Secondary accession number(s): P04384, P30869, Q2M9Q1
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: January 23, 2007
    Last modified: November 13, 2019
    This is version 134 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again