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P0A817

- METK_ECOLI

UniProt

P0A817 - METK_ECOLI

Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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      Entry version 100 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
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    Functioni

    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.

    Catalytic activityi

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

    Cofactori

    Binds 2 divalent ions per subunit. Magnesium or cobalt.
    Binds 1 potassium ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi17 – 171Magnesium
    Metal bindingi43 – 431Potassium
    Binding sitei119 – 1191Methionine
    Binding sitei239 – 2391Methionine
    Metal bindingi264 – 2641Potassium
    Metal bindingi272 – 2721Magnesium

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi260 – 2678ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. identical protein binding Source: IntAct
    3. magnesium ion binding Source: EcoCyc
    4. methionine adenosyltransferase activity Source: EcoCyc
    5. potassium ion binding Source: EcoCyc
    6. protein binding Source: IntAct

    GO - Biological processi

    1. one-carbon metabolic process Source: UniProtKB-HAMAP
    2. S-adenosylmethionine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

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

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine synthase (EC:2.5.1.6)
    Short name:
    AdoMet synthase
    Alternative name(s):
    MAT
    Methionine adenosyltransferase
    Gene namesi
    Name:metK
    Synonyms:metX
    Ordered Locus Names:b2942, JW2909
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10589. metK.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151H → N: Loss of activity. 1 Publication
    Mutagenesisi17 – 171D → N or A: Loss of activity. 1 Publication
    Mutagenesisi43 – 431E → K: Misfolding and subject to proteolytic degradation. 1 Publication
    Mutagenesisi43 – 431E → Q: Loss of stimulation by potassium. 1 Publication
    Mutagenesisi90 – 901C → A or S: Decrease in the homotetramer formation capability. Enhanced thermal stability. 1 Publication
    Mutagenesisi119 – 1191D → N: Decrease of both AdoMet synthesis and AdoMet-activated tripolyphosphate hydrolysis. 1 Publication
    Mutagenesisi166 – 1661K → M: Decrease in AdoMet synthesis. 1 Publication
    Mutagenesisi239 – 2391D → N: Decrease in AdoMet synthesis. 1 Publication
    Mutagenesisi240 – 2401C → A: Decrease in AdoMet synthesis. 1 Publication
    Mutagenesisi245 – 2451R → H or L: Loss of activity. 1 Publication
    Mutagenesisi246 – 2461K → M: Loss of activity. modification in protein conformation. 1 Publication
    Mutagenesisi266 – 2661K → A: Loss of activity. 1 Publication
    Mutagenesisi266 – 2661K → M: Unstable; trace activity. 1 Publication
    Mutagenesisi270 – 2701K → M: Decrease in activity. 1 Publication
    Mutagenesisi272 – 2721D → N or A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 384383S-adenosylmethionine synthasePRO_0000174518Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A817.
    PRIDEiP0A817.

    2D gel databases

    SWISS-2DPAGEP0A817.

    PTM databases

    PhosSiteiP0809415.

    Expressioni

    Inductioni

    AdoMet activates the tripolyphosphatase reaction.

    Gene expression databases

    GenevestigatoriP0A817.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

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

    Protein-protein interaction databases

    DIPiDIP-35672N.
    IntActiP0A817. 38 interactions.
    MINTiMINT-1233798.
    STRINGi511145.b2942.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Helixi16 – 3419
    Beta strandi39 – 479
    Beta strandi50 – 589
    Helixi65 – 7612
    Helixi81 – 833
    Turni87 – 893
    Beta strandi90 – 978
    Helixi101 – 1077
    Turni112 – 1143
    Beta strandi117 – 1193
    Beta strandi121 – 1288
    Helixi137 – 15418
    Beta strandi156 – 1583
    Beta strandi161 – 17414
    Beta strandi177 – 19014
    Beta strandi192 – 1943
    Helixi196 – 20611
    Turni207 – 2115
    Helixi214 – 2163
    Beta strandi222 – 2265
    Helixi235 – 2384
    Beta strandi239 – 2424
    Turni247 – 2548
    Helixi271 – 28818
    Beta strandi291 – 30111
    Beta strandi309 – 3146
    Beta strandi319 – 3213
    Helixi323 – 33311
    Helixi338 – 3458
    Beta strandi348 – 3503
    Helixi353 – 3564
    Beta strandi360 – 3623
    Beta strandi364 – 3663
    Turni367 – 3693
    Helixi373 – 3797
    Turni380 – 3823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A817.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni239 – 24810Pyrophosphate binding

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0192.
    HOGENOMiHOG000245710.
    KOiK00789.
    OMAiGYVNSEM.
    OrthoDBiEOG68WR6M.
    PhylomeDBiP0A817.

    Family and domain databases

    HAMAPiMF_00086. S_AdoMet_synth1.
    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

    MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM    50
    VLVGGEITTS AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS 100
    PDINQGVDRA DPLEQGAGDQ GLMFGYATNE TDVLMPAPIT YAHRLVQRQA 150
    EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG IDAVVLSTQH SEEIDQKSLQ 200
    EAVMEEIIKP ILPAEWLTSA TKFFINPTGR FVIGGPMGDC GLTGRKIIVD 250
    TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS 300
    YAIGVAEPTS IMVETFGTEK VPSEQLTLLV REFFDLRPYG LIQMLDLLHP 350
    IYKETAAYGH FGREHFPWEK TDKAQLLRDA AGLK 384
    Length:384
    Mass (Da):41,952
    Last modified:January 23, 2007 - v2
    Checksum:i97FA8CF17B542941
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 6112MVLVG…ITTSA → IGFSWRRNHHQRP(PubMed:6094561)CuratedAdd
    BLAST
    Sequence conflicti50 – 6112MVLVG…ITTSA → IGFSWRRNHHQRP(PubMed:2198270)CuratedAdd
    BLAST
    Sequence conflicti123 – 13311MFGYATNETDV → DVSATQLMKPTC in AAA24164. (PubMed:6094561)CuratedAdd
    BLAST
    Sequence conflicti159 – 1613PWL → RV(PubMed:6094561)Curated
    Sequence conflicti159 – 1613PWL → RV(PubMed:8231813)Curated
    Sequence conflicti172 – 1721Q → S in AAA24164. (PubMed:6094561)Curated
    Sequence conflicti252 – 2521Y → T in AAA24164. (PubMed:6094561)Curated
    Sequence conflicti305 – 3051V → L in AAA24164. (PubMed:6094561)Curated
    Sequence conflicti337 – 3371Missing(PubMed:6094561)Curated
    Sequence conflicti339 – 3391Y → I(PubMed:6094561)Curated
    Sequence conflicti375 – 3762QL → HV(PubMed:8231813)Curated
    Sequence conflicti378 – 3781R → P(PubMed:8231813)Curated

    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
    GenBank
    DDBJ
    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.
    YP_491141.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75979; AAC75979; b2942.
    BAE77005; BAE77005; BAE77005.
    GeneIDi12931663.
    945389.
    KEGGiecj:Y75_p2872.
    eco:b2942.
    PATRICi32121294. VBIEscCol129921_3035.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02129 Genomic DNA. Translation: AAA24164.1 .
    U28377 Genomic DNA. Translation: AAA69109.1 .
    U00096 Genomic DNA. Translation: AAC75979.1 .
    AP009048 Genomic DNA. Translation: BAE77005.1 .
    M98266 Genomic DNA. Translation: AAB05197.1 .
    M31770 Genomic DNA. Translation: AAA24645.2 .
    PIRi E65079. SYECSM.
    RefSeqi NP_417417.1. NC_000913.3.
    YP_491141.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FUG X-ray 3.20 A/B 2-384 [» ]
    1MXA X-ray 2.80 A 2-384 [» ]
    1MXB X-ray 2.80 A 2-384 [» ]
    1MXC X-ray 3.00 A 2-384 [» ]
    1P7L X-ray 2.50 A/B/C/D 2-384 [» ]
    1RG9 X-ray 2.50 A/B/C/D 2-384 [» ]
    1XRA X-ray 3.00 A 2-384 [» ]
    1XRB X-ray 3.00 A 2-384 [» ]
    1XRC X-ray 3.00 A 2-384 [» ]
    ProteinModelPortali P0A817.
    SMRi P0A817. Positions 2-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35672N.
    IntActi P0A817. 38 interactions.
    MINTi MINT-1233798.
    STRINGi 511145.b2942.

    PTM databases

    PhosSitei P0809415.

    2D gel databases

    SWISS-2DPAGE P0A817.

    Proteomic databases

    PaxDbi P0A817.
    PRIDEi P0A817.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75979 ; AAC75979 ; b2942 .
    BAE77005 ; BAE77005 ; BAE77005 .
    GeneIDi 12931663.
    945389.
    KEGGi ecj:Y75_p2872.
    eco:b2942.
    PATRICi 32121294. VBIEscCol129921_3035.

    Organism-specific databases

    EchoBASEi EB0584.
    EcoGenei EG10589. metK.

    Phylogenomic databases

    eggNOGi COG0192.
    HOGENOMi HOG000245710.
    KOi K00789.
    OMAi GYVNSEM.
    OrthoDBi EOG68WR6M.
    PhylomeDBi P0A817.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    BioCyci EcoCyc:S-ADENMETSYN-MONOMER.
    ECOL316407:JW2909-MONOMER.
    MetaCyc:S-ADENMETSYN-MONOMER.
    SABIO-RK P0A817.

    Miscellaneous databases

    EvolutionaryTracei P0A817.
    PROi P0A817.

    Gene expression databases

    Genevestigatori P0A817.

    Family and domain databases

    HAMAPi MF_00086. S_AdoMet_synth1.
    InterProi 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.
    [Graphical view ]
    PANTHERi PTHR11964. PTHR11964. 1 hit.
    Pfami PF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000497. MAT. 1 hit.
    SUPFAMi SSF55973. SSF55973. 3 hits.
    TIGRFAMsi TIGR01034. metK. 1 hit.
    PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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).

    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: October 1, 2014
    This is version 100 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

    External Data

    Dasty 3