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Entry version 145 (23 Feb 2022)
Sequence version 2 (23 Jan 2007)
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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

<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%5Fsection">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%5Fsection">'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 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%5Fsection">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%5Fsection">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%5Fsection">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

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

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%5Fand%5Fbiotech%5Fsection">'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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0A817

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

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PaxDbi
P0A817

PRoteomics IDEntifications database

More...
PRIDEi
P0A817

2D gel databases

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

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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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
4260657, 257 interactors

Database of interacting proteins

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DIPi
DIP-35672N

Protein interaction database and analysis system

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IntActi
P0A817, 39 interactors

Molecular INTeraction database

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MINTi
P0A817

STRING: functional protein association networks

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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

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SMRi
P0A817

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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
COG0192, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_041802_1_1_6

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0A817

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

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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

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PIRSFi
PIRSF000497, MAT, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55973, SSF55973, 3 hits

TIGRFAMs; a protein family database

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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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

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PIRi
E65079, SYECSM

NCBI Reference Sequences

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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

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GeneIDi
66673177
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

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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

jPOSTiP0A817
PaxDbiP0A817
PRIDEiP0A817

Genome annotation databases

EnsemblBacteriaiAAC75979; AAC75979; b2942
BAE77005; BAE77005; BAE77005
GeneIDi66673177
945389
KEGGiecj:JW2909
eco:b2942
PATRICifig|1411691.4.peg.3791

Organism-specific databases

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

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EchoBASEi
EB0584

Phylogenomic databases

eggNOGiCOG0192, Bacteria
HOGENOMiCLU_041802_1_1_6
InParanoidiP0A817
PhylomeDBiP0A817

Enzyme and pathway databases

UniPathwayiUPA00315;UER00080
BioCyciEcoCyc:S-ADENMETSYN-MONOMER
BRENDAi2.5.1.6, 2026
SABIO-RKiP0A817

Miscellaneous databases

EvolutionaryTraceiP0A817

Protein Ontology

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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

MobiDB: a database of protein disorder and mobility annotations

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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%5Fand%5Fisoforms">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: February 23, 2022
This is version 145 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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