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P25665

- METE_ECOLI

UniProt

P25665 - METE_ECOLI

Protein

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Gene

metE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 6 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

    Catalytic activityi

    5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.

    Cofactori

    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi641 – 6411Zinc
    Metal bindingi643 – 6431Zinc
    Metal bindingi726 – 7261Zinc

    GO - Molecular functioni

    1. 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Source: EcoCyc
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. methionine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:HOMOCYSMET-MONOMER.
    ECOL316407:JW3805-MONOMER.
    MetaCyc:HOMOCYSMET-MONOMER.
    BRENDAi2.1.1.14. 2026.
    UniPathwayiUPA00051; UER00082.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC:2.1.1.14)
    Alternative name(s):
    Cobalamin-independent methionine synthase
    Methionine synthase, vitamin-B12 independent isozyme
    Gene namesi
    Name:metE
    Ordered Locus Names:b3829, JW3805
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10584. metE.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi641 – 6411H → N: Impaired activity, lower affinity for zinc binding. 1 Publication
    Mutagenesisi641 – 6411H → Q: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. 1 Publication
    Mutagenesisi643 – 6431C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 7x tighter than wild-type. 1 Publication
    Mutagenesisi726 – 7261C → S: Impaired activity, lower affinity for zinc binding. Binds homocysteine 2-4x more weakly than wild-type. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 7537525-methyltetrahydropteroyltriglutamate--homocysteine methyltransferasePRO_0000098630Add
    BLAST

    Proteomic databases

    PaxDbiP25665.
    PRIDEiP25665.

    Expressioni

    Gene expression databases

    GenevestigatoriP25665.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    uvrDP030182EBI-551247,EBI-559573

    Protein-protein interaction databases

    DIPiDIP-6847N.
    IntActiP25665. 11 interactions.
    MINTiMINT-1280694.
    STRINGi511145.b3829.

    Structurei

    3D structure databases

    ProteinModelPortaliP25665.
    SMRiP25665. Positions 3-751.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati2 – 370369ApproximateAdd
    BLAST
    Repeati371 – 753383ApproximateAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0620.
    HOGENOMiHOG000246221.
    KOiK00549.
    OMAiFKANPAH.
    OrthoDBiEOG6FFS3G.
    PhylomeDBiP25665.

    Family and domain databases

    HAMAPiMF_00172. Meth_synth.
    InterProiIPR013215. Cbl-indep_Met_Synth_N.
    IPR006276. Cobalamin-indep_Met_synthase.
    IPR002629. Met_Synth_C/arc.
    [Graphical view]
    PfamiPF08267. Meth_synt_1. 1 hit.
    PF01717. Meth_synt_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
    TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P25665-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLAVG RELRARHWDQ    50
    QKQAGIDLLP VGDFAWYDHV LTTSLLLGNV PARHQNKDGS VDIDTLFRIG 100
    RGRAPTGEPA AAAEMTKWFN TNYHYMVPEF VKGQQFKLTW TQLLDEVDEA 150
    LALGHKVKPV LLGPVTWLWL GKVKGEQFDR LSLLNDILPV YQQVLAELAK 200
    RGIEWVQIDE PALVLELPQA WLDAYKPAYD ALQGQVKLLL TTYFEGVTPN 250
    LDTITALPVQ GLHVDLVHGK DDVAELHKRL PSDWLLSAGL INGRNVWRAD 300
    LTEKYAQIKD IVGKRDLWVA SSCSLLHSPI DLSVETRLDA EVKSWFAFAL 350
    QKCHELALLR DALNSGDTAA LAEWSAPIQA RRHSTRVHNP AVEKRLAAIT 400
    AQDSQRANVY EVRAEAQRAR FKLPAWPTTT IGSFPQTTEI RTLRLDFKKG 450
    NLDANNYRTG IAEHIKQAIV EQERLGLDVL VHGEAERNDM VEYFGEHLDG 500
    FVFTQNGWVQ SYGSRCVKPP IVIGDISRPA PITVEWAKYA QSLTDKPVKG 550
    MLTGPVTILC WSFPREDVSR ETIAKQIALA LRDEVADLEA AGIGIIQIDE 600
    PALREGLPLR RSDWDAYLQW GVEAFRINAA VAKDDTQIHT HMCYCEFNDI 650
    MDSIAALDAD VITIETSRSD MELLESFEEF DYPNEIGPGV YDIHSPNVPS 700
    VEWIEALLKK AAKRIPAERL WVNPDCGLKT RGWPETRAAL ANMVQAAQNL 750
    RRG 753
    Length:753
    Mass (Da):84,674
    Last modified:January 23, 2007 - v6
    Checksum:iC46BE52F227AFAF1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti363 – 3631L → V in AAA23544. (PubMed:1339288)Curated
    Sequence conflicti605 – 6051E → Q in AAA67625. (PubMed:8346018)Curated
    Sequence conflicti659 – 6591A → R in AAA67625. (PubMed:8346018)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87625 Genomic DNA. Translation: AAA23544.1.
    M87049 Genomic DNA. Translation: AAA67625.1.
    U00096 Genomic DNA. Translation: AAC76832.1.
    AP009048 Genomic DNA. Translation: BAE77472.1.
    J04155 Genomic DNA. Translation: AAA24160.1.
    PIRiF65187. A42863.
    RefSeqiNP_418273.1. NC_000913.3.
    YP_491613.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76832; AAC76832; b3829.
    BAE77472; BAE77472; BAE77472.
    GeneIDi12930483.
    948323.
    KEGGiecj:Y75_p3349.
    eco:b3829.
    PATRICi32123159. VBIEscCol129921_3945.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87625 Genomic DNA. Translation: AAA23544.1 .
    M87049 Genomic DNA. Translation: AAA67625.1 .
    U00096 Genomic DNA. Translation: AAC76832.1 .
    AP009048 Genomic DNA. Translation: BAE77472.1 .
    J04155 Genomic DNA. Translation: AAA24160.1 .
    PIRi F65187. A42863.
    RefSeqi NP_418273.1. NC_000913.3.
    YP_491613.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P25665.
    SMRi P25665. Positions 3-751.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6847N.
    IntActi P25665. 11 interactions.
    MINTi MINT-1280694.
    STRINGi 511145.b3829.

    Proteomic databases

    PaxDbi P25665.
    PRIDEi P25665.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76832 ; AAC76832 ; b3829 .
    BAE77472 ; BAE77472 ; BAE77472 .
    GeneIDi 12930483.
    948323.
    KEGGi ecj:Y75_p3349.
    eco:b3829.
    PATRICi 32123159. VBIEscCol129921_3945.

    Organism-specific databases

    EchoBASEi EB0579.
    EcoGenei EG10584. metE.

    Phylogenomic databases

    eggNOGi COG0620.
    HOGENOMi HOG000246221.
    KOi K00549.
    OMAi FKANPAH.
    OrthoDBi EOG6FFS3G.
    PhylomeDBi P25665.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00082 .
    BioCyci EcoCyc:HOMOCYSMET-MONOMER.
    ECOL316407:JW3805-MONOMER.
    MetaCyc:HOMOCYSMET-MONOMER.
    BRENDAi 2.1.1.14. 2026.

    Miscellaneous databases

    PROi P25665.

    Gene expression databases

    Genevestigatori P25665.

    Family and domain databases

    HAMAPi MF_00172. Meth_synth.
    InterProi IPR013215. Cbl-indep_Met_Synth_N.
    IPR006276. Cobalamin-indep_Met_synthase.
    IPR002629. Met_Synth_C/arc.
    [Graphical view ]
    Pfami PF08267. Meth_synt_1. 1 hit.
    PF01717. Meth_synt_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000382. MeTrfase_B12_ind. 1 hit.
    TIGRFAMsi TIGR01371. met_syn_B12ind. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem."
      Gonzalez J.C., Banerjee R.V., Huang S., Sumner J.S., Matthews R.G.
      Biochemistry 31:6045-6056(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12 / DH5-alpha.
    2. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 604 AND 658.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Regulation of methionine synthesis in Escherichia coli: effect of the MetR protein on the expression of the metE and metR genes."
      Maxon M.E., Redfield B., Cai X.-Y., Shoeman R., Fujita K., Fisher W., Stauffer G., Weissbach H., Brot N.
      Proc. Natl. Acad. Sci. U.S.A. 86:85-89(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    8. "Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme."
      Gonzalez J.C., Peariso K., Penner-Hahn J.E., Matthews R.G.
      Biochemistry 35:12228-12234(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF CYS-726.
    9. "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.
    10. "Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli."
      Zhou Z.S., Peariso K., Penner-Hahn J.E., Matthews R.G.
      Biochemistry 38:15915-15926(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-641; CYS-643 AND CYS-726.

    Entry informationi

    Entry nameiMETE_ECOLI
    AccessioniPrimary (citable) accession number: P25665
    Secondary accession number(s): Q2M8D4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has an absolute requirement for a polyglutamylated folate as substrate. Its activity depends on phosphate anions and divalent cations.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3