Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A817 (METK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine synthase

Short name=AdoMet synthase
EC=2.5.1.6
Alternative name(s):
MAT
Methionine adenosyltransferase
Gene names
Name:metK
Synonyms:metX
Ordered Locus Names:b2942, JW2909
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of S-adenosylmethionine 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. Is essential for growth. HAMAP-Rule MF_00086

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP-Rule MF_00086

Cofactor

Binds 2 divalent ions per subunit. Magnesium or cobalt.

Binds 1 potassium ion per subunit.

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP-Rule MF_00086

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00086.

Induction

AdoMet activates the tripolyphosphatase reaction. HAMAP-Rule MF_00086

Disruption phenotype

Cells are resistant to methionine-analogs, such as DL-ethionine(Et). Ref.2

Sequence similarities

Belongs to the AdoMet synthase family.

Caution

Was originally (Ref.2) thought to differ from MetX, which was assigned as a second AdoMet synthase before being shown to be identical to MetK.

Mass spectrometry

Molecular mass is 41843±10.5 Da from positions 2 - 384. Determined by ESI. Ref.14

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-546295,EBI-546295
groLP0A6F52EBI-546295,EBI-543750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00086
Chain2 – 384383S-adenosylmethionine synthase HAMAP-Rule MF_00086
PRO_0000174518

Regions

Nucleotide binding260 – 2678ATP Potential
Region239 – 24810Pyrophosphate binding HAMAP-Rule MF_00086

Sites

Metal binding171Magnesium
Metal binding431Potassium
Metal binding2641Potassium
Metal binding2721Magnesium
Binding site1191Methionine
Binding site2391Methionine

Amino acid modifications

Modified residue31N6-acetyllysine Ref.13

Experimental info

Mutagenesis151H → N: Loss of activity. Ref.11
Mutagenesis171D → N or A: Loss of activity. Ref.10
Mutagenesis431E → K: Misfolding and subject to proteolytic degradation. Ref.6
Mutagenesis431E → Q: Loss of stimulation by potassium. Ref.6
Mutagenesis901C → A or S: Decrease in the homotetramer formation capability. Enhanced thermal stability. Ref.7
Mutagenesis1191D → N: Decrease of both AdoMet synthesis and AdoMet-activated tripolyphosphate hydrolysis. Ref.10
Mutagenesis1661K → M: Decrease in AdoMet synthesis. Ref.11
Mutagenesis2391D → N: Decrease in AdoMet synthesis. Ref.10
Mutagenesis2401C → A: Decrease in AdoMet synthesis. Ref.7
Mutagenesis2451R → H or L: Loss of activity. Ref.9
Mutagenesis2461K → M: Loss of activity. modification in protein conformation. Ref.11
Mutagenesis2661K → A: Loss of activity. Ref.11
Mutagenesis2661K → M: Unstable; trace activity. Ref.11
Mutagenesis2701K → M: Decrease in activity. Ref.11
Mutagenesis2721D → N or A: Loss of activity. Ref.10
Sequence conflict50 – 6112MVLVG…ITTSA → IGFSWRRNHHQRP Ref.1
Sequence conflict50 – 6112MVLVG…ITTSA → IGFSWRRNHHQRP Ref.5
Sequence conflict123 – 13311MFGYATNETDV → DVSATQLMKPTC in AAA24164. Ref.1
Sequence conflict159 – 1613PWL → RV Ref.1
Sequence conflict159 – 1613PWL → RV Ref.2
Sequence conflict1721Q → S in AAA24164. Ref.1
Sequence conflict2521Y → T in AAA24164. Ref.1
Sequence conflict3051V → L in AAA24164. Ref.1
Sequence conflict3371Missing Ref.1
Sequence conflict3391Y → I Ref.1
Sequence conflict375 – 3762QL → HV Ref.2
Sequence conflict3781R → P Ref.2

Secondary structure

...................................................................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A817 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 97FA8CF17B542941

FASTA38441,952
        10         20         30         40         50         60 
MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS 

        70         80         90        100        110        120 
AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS PDINQGVDRA DPLEQGAGDQ 

       130        140        150        160        170        180 
GLMFGYATNE TDVLMPAPIT YAHRLVQRQA EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG 

       190        200        210        220        230        240 
IDAVVLSTQH SEEIDQKSLQ EAVMEEIIKP ILPAEWLTSA TKFFINPTGR FVIGGPMGDC 

       250        260        270        280        290        300 
GLTGRKIIVD TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS 

       310        320        330        340        350        360 
YAIGVAEPTS IMVETFGTEK VPSEQLTLLV REFFDLRPYG LIQMLDLLHP IYKETAAYGH 

       370        380 
FGREHFPWEK TDKAQLLRDA AGLK 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli."
Markham G.D., Deparasis J., Gatmaitan J.
J. Biol. Chem. 259:14505-14507(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isozymes of S-adenosylmethionine synthetase are encoded by tandemly duplicated genes in Escherichia coli."
Satishchandran C., Taylor J.C., Markham G.D.
Mol. Microbiol. 9:835-846(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli."
Moore R.C., Boyle S.M.
J. Bacteriol. 172:4631-4640(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
[6]"Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition."
McQueney M.S., Markham G.D.
J. Biol. Chem. 270:18277-18284(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-43.
[7]"Structural and functional roles of cysteine 90 and cysteine 240 in S-adenosylmethionine synthetase."
Reczkowski R.S., Markham G.D.
J. Biol. Chem. 270:18484-18490(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-90 AND CYS-240.
Strain: B and K12.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"The active-site arginine of S-adenosylmethionine synthetase orients the reaction intermediate."
Reczkowski R.S., Taylor J.C., Markham G.D.
Biochemistry 37:13499-13506(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-245.
Strain: B and K12.
[10]"The bifunctional active site of S-adenosylmethionine synthetase. Roles of the active site aspartates."
Taylor J.C., Markham G.D.
J. Biol. Chem. 274:32909-32914(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-17; ASP-119; ASP-239 AND ASP-272.
Strain: B and K12.
[11]"The bifunctional active site of S-adenosylmethionine synthetase. Roles of the basic residues."
Taylor J.C., Markham G.D.
J. Biol. Chem. 275:4060-4065(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-15; LYS-166; LYS-246; LYS-266 AND LYS-270.
Strain: B and K12.
[12]"Studies on the role of the metK gene product of Escherichia coli K-12."
Wei Y., Newman E.B.
Mol. Microbiol. 43:1651-1656(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL START SITE, ESSENTIAL GENE.
[13]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[14]"Crystal structure of S-adenosylmethionine synthetase."
Takusagawa F., Kamitori S., Misaki S., Markham G.D.
J. Biol. Chem. 271:136-147(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), MASS SPECTROMETRY.
[15]"Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 2.8-A resolution."
Takusagawa F., Kamitori S., Markham G.D.
Biochemistry 35:2586-2596(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]"Flexible loop in the structure of S-adenosylmethionine synthetase crystallized in the tetragonal modification."
Fu Z., Hu Y., Markham G.D., Takusagawa F.
J. Biomol. Struct. Dyn. 13:727-739(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRSYECSM. E65079.
RefSeqNP_417417.1. NC_000913.3.
YP_491141.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A817.
SMRP0A817. Positions 2-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35672N.
IntActP0A817. 38 interactions.
MINTMINT-1233798.
STRING511145.b2942.

PTM databases

PhosSiteP0809415.

2D gel databases

SWISS-2DPAGEP0A817.

Proteomic databases

PaxDbP0A817.
PRIDEP0A817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75979; AAC75979; b2942.
BAE77005; BAE77005; BAE77005.
GeneID12931663.
945389.
KEGGecj:Y75_p2872.
eco:b2942.
PATRIC32121294. VBIEscCol129921_3035.

Organism-specific databases

EchoBASEEB0584.
EcoGeneEG10589. metK.

Phylogenomic databases

eggNOGCOG0192.
HOGENOMHOG000245710.
KOK00789.
OMAGYVNSEM.
OrthoDBEOG68WR6M.
PhylomeDBP0A817.

Enzyme and pathway databases

BioCycEcoCyc:S-ADENMETSYN-MONOMER.
ECOL316407:JW2909-MONOMER.
MetaCyc:S-ADENMETSYN-MONOMER.
SABIO-RKP0A817.
UniPathwayUPA00315; UER00080.

Gene expression databases

GenevestigatorP0A817.

Family and domain databases

HAMAPMF_00086. S_AdoMet_synth1.
InterProIPR022631. 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]
PANTHERPTHR11964. PTHR11964. 1 hit.
PfamPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000497. MAT. 1 hit.
SUPFAMSSF55973. SSF55973. 3 hits.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A817.
PROP0A817.

Entry information

Entry nameMETK_ECOLI
AccessionPrimary (citable) accession number: P0A817
Secondary accession number(s): P04384, P30869, Q2M9Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene