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P13009

- METH_ECOLI

UniProt

P13009 - METH_ECOLI

Protein

Methionine synthase

Gene

metH

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 154 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

    Catalytic activityi

    5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

    Cofactori

    Methylcobalamin (MeCBL).
    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi247 – 2471Zinc
    Metal bindingi310 – 3101Zinc
    Metal bindingi311 – 3111Zinc
    Metal bindingi759 – 7591Cobalt (cobalamin axial ligand)1 Publication
    Binding sitei804 – 8041Cobalamin2 Publications
    Binding sitei946 – 9461S-adenosyl-L-methionine1 Publication
    Binding sitei1134 – 11341S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
    Binding sitei1138 – 11381Cobalamin; via carbonyl oxygen2 Publications

    GO - Molecular functioni

    1. cobalamin binding Source: EcoCyc
    2. methionine synthase activity Source: EcoCyc
    3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: EcoCyc
    4. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. pteridine-containing compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:HOMOCYSMETB12-MONOMER.
    ECOL316407:JW3979-MONOMER.
    MetaCyc:HOMOCYSMETB12-MONOMER.
    RETL1328306-WGS:GSTH-2949-MONOMER.
    UniPathwayiUPA00051; UER00081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine synthase (EC:2.1.1.13)
    Alternative name(s):
    5-methyltetrahydrofolate--homocysteine methyltransferase
    Methionine synthase, vitamin-B12-dependent
    Short name:
    MS
    Gene namesi
    Name:metH
    Ordered Locus Names:b4019, JW3979
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10587. metH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi310 – 3101C → A or S: Loss of zinc binding. Loss of catalytic activity. 1 Publication
    Mutagenesisi311 – 3111C → A or S: Loss of zinc binding. Loss of catalytic activity. 1 Publication
    Mutagenesisi757 – 7571D → E: Decreases activity by about 70%. 1 Publication
    Mutagenesisi757 – 7571D → N: Decreases activity by about 45%. 1 Publication
    Mutagenesisi759 – 7591H → G: Loss of catalytic activity. 1 Publication
    Mutagenesisi810 – 8101S → A: Decreases activity by about 40%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 12271226Methionine synthasePRO_0000204532Add
    BLAST

    Proteomic databases

    PaxDbiP13009.
    PRIDEiP13009.

    2D gel databases

    SWISS-2DPAGEP13009.

    Expressioni

    Gene expression databases

    GenevestigatoriP13009.

    Interactioni

    Protein-protein interaction databases

    IntActiP13009. 13 interactions.
    STRINGi511145.b4019.

    Structurei

    Secondary structure

    1
    1227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi653 – 6564
    Helixi659 – 66911
    Helixi675 – 68511
    Beta strandi686 – 6883
    Helixi691 – 6944
    Helixi696 – 71015
    Helixi715 – 73723
    Beta strandi738 – 7414
    Beta strandi748 – 7547
    Helixi761 – 77111
    Turni772 – 7743
    Beta strandi776 – 7794
    Beta strandi782 – 7843
    Helixi786 – 79611
    Beta strandi799 – 8046
    Helixi809 – 82315
    Beta strandi830 – 8345
    Beta strandi835 – 8373
    Helixi839 – 8457
    Helixi847 – 8493
    Beta strandi854 – 8563
    Helixi860 – 87011
    Turni873 – 8753
    Helixi876 – 89318
    Helixi906 – 9116
    Helixi918 – 9203
    Beta strandi930 – 9356
    Helixi938 – 9414
    Helixi942 – 9443
    Helixi948 – 9536
    Helixi962 – 9654
    Turni967 – 9693
    Helixi970 – 99021
    Beta strandi996 – 100712
    Beta strandi1010 – 10167
    Beta strandi1022 – 10276
    Beta strandi1036 – 10383
    Helixi1043 – 10464
    Helixi1050 – 10523
    Beta strandi1057 – 10659
    Helixi1069 – 107810
    Helixi1082 – 110928
    Helixi1122 – 11265
    Beta strandi1130 – 11334
    Helixi1145 – 11473
    Helixi1148 – 11547
    Helixi1157 – 11615
    Beta strandi1167 – 11693
    Beta strandi1171 – 118212
    Helixi1197 – 120711
    Helixi1211 – 12188
    Helixi1219 – 12213
    Beta strandi1222 – 12243

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BMTX-ray3.00A/B651-896[»]
    1K7YX-ray3.00A651-1227[»]
    1K98X-ray3.75A651-1227[»]
    1MSKX-ray1.80A897-1227[»]
    3BULX-ray2.30A649-1227[»]
    3IV9X-ray3.25A649-1227[»]
    3IVAX-ray2.70A649-1227[»]
    ProteinModelPortaliP13009.
    SMRiP13009. Positions 6-639, 651-1227.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13009.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 325324Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 617262Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini650 – 74495B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini746 – 881136B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini897 – 1227331AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni834 – 8352Cobalamin-binding
    Regioni1189 – 11902S-adenosyl-L-methionine binding

    Domaini

    Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.1 Publication

    Sequence similaritiesi

    Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
    Contains 1 B12-binding domain.PROSITE-ProRule annotation
    Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1410.
    HOGENOMiHOG000251409.
    KOiK00548.
    OMAiLTEHYAM.
    OrthoDBiEOG6091CH.
    PhylomeDBiP13009.

    Family and domain databases

    Gene3Di1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProiIPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view]
    PfamiPF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000381. MetH. 1 hit.
    SMARTiSM01018. B12-binding_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsiTIGR02082. metH. 1 hit.
    PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13009-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK     50
    GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS 100
    AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA 150
    FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF 200
    EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG 250
    PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ 300
    AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI 350
    GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI 400
    NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG 450
    KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI 500
    CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK 550
    RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG 600
    QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ 650
    QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG 700
    MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV 750
    IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL 800
    IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY 850
    SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR 900
    TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF 950
    FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG 1000
    LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK 1050
    LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA 1100
    EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT 1150
    IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV 1200
    EDYARRKGMS VTEVERWLAP NLGYDAD 1227
    Length:1,227
    Mass (Da):135,997
    Last modified:January 23, 2007 - v5
    Checksum:i91F0CAA1E9127D9A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131A → R(PubMed:2185137)Curated
    Sequence conflicti113 – 1131A → R(PubMed:2668277)Curated
    Sequence conflicti641 – 6411S → T(PubMed:2185137)Curated
    Sequence conflicti641 – 6411S → T(PubMed:2668277)Curated
    Sequence conflicti1079 – 10802QH → HD in CAA34601. (PubMed:2185137)Curated
    Sequence conflicti1195 – 122733IQRDQ…GYDAD → TSARSG in CAA34601. (PubMed:2185137)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16584 Genomic DNA. Translation: CAA34601.1.
    J04975 Unassigned DNA. Translation: AAA02995.1.
    U00006 Genomic DNA. Translation: AAC43113.1.
    U00096 Genomic DNA. Translation: AAC76989.1.
    AP009048 Genomic DNA. Translation: BAE78021.1.
    PIRiB65209. XYECMH.
    RefSeqiNP_418443.1. NC_000913.3.
    YP_492162.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76989; AAC76989; b4019.
    BAE78021; BAE78021; BAE78021.
    GeneIDi12934458.
    948522.
    KEGGiecj:Y75_p3906.
    eco:b4019.
    PATRICi32123567. VBIEscCol129921_4132.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16584 Genomic DNA. Translation: CAA34601.1 .
    J04975 Unassigned DNA. Translation: AAA02995.1 .
    U00006 Genomic DNA. Translation: AAC43113.1 .
    U00096 Genomic DNA. Translation: AAC76989.1 .
    AP009048 Genomic DNA. Translation: BAE78021.1 .
    PIRi B65209. XYECMH.
    RefSeqi NP_418443.1. NC_000913.3.
    YP_492162.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BMT X-ray 3.00 A/B 651-896 [» ]
    1K7Y X-ray 3.00 A 651-1227 [» ]
    1K98 X-ray 3.75 A 651-1227 [» ]
    1MSK X-ray 1.80 A 897-1227 [» ]
    3BUL X-ray 2.30 A 649-1227 [» ]
    3IV9 X-ray 3.25 A 649-1227 [» ]
    3IVA X-ray 2.70 A 649-1227 [» ]
    ProteinModelPortali P13009.
    SMRi P13009. Positions 6-639, 651-1227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13009. 13 interactions.
    STRINGi 511145.b4019.

    2D gel databases

    SWISS-2DPAGE P13009.

    Proteomic databases

    PaxDbi P13009.
    PRIDEi P13009.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76989 ; AAC76989 ; b4019 .
    BAE78021 ; BAE78021 ; BAE78021 .
    GeneIDi 12934458.
    948522.
    KEGGi ecj:Y75_p3906.
    eco:b4019.
    PATRICi 32123567. VBIEscCol129921_4132.

    Organism-specific databases

    EchoBASEi EB0582.
    EcoGenei EG10587. metH.

    Phylogenomic databases

    eggNOGi COG1410.
    HOGENOMi HOG000251409.
    KOi K00548.
    OMAi LTEHYAM.
    OrthoDBi EOG6091CH.
    PhylomeDBi P13009.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .
    BioCyci EcoCyc:HOMOCYSMETB12-MONOMER.
    ECOL316407:JW3979-MONOMER.
    MetaCyc:HOMOCYSMETB12-MONOMER.
    RETL1328306-WGS:GSTH-2949-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P13009.
    PROi P13009.

    Gene expression databases

    Genevestigatori P13009.

    Family and domain databases

    Gene3Di 1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProi IPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view ]
    Pfami PF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000381. MetH. 1 hit.
    SMARTi SM01018. B12-binding_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsi TIGR02082. metH. 1 hit.
    PROSITEi PS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2."
      Old I.G., Margarita D., Glass R.E., Saint-Girons I.
      Gene 87:15-21(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain."
      Banerjee R.V., Johnston N.L., Sobeski J.K., Datta P., Matthews R.G.
      J. Biol. Chem. 264:13888-13895(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12.
    3. "Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase."
      Drummond J.T., Loo R.R., Matthews R.G.
      Biochemistry 32:9282-9289(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.
    7. "Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine."
      Goulding C.W., Postigo D., Matthews R.G.
      Biochemistry 36:8082-8091(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION, DOMAIN, MUTAGENESIS OF CYS-310 AND CYS-311.
      Strain: K12.
    8. "Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli."
      Luschinsky C.L., Drummond J.T., Matthews R.G., Ludwig M.L.
      J. Mol. Biol. 225:557-560(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    9. "Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity."
      Jarrett J.T., Amaratunga M., Drennan C.L., Scholten J.D., Sands R.H., Ludwig M.L., Matthews R.G.
      Biochemistry 35:2464-2475(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-757; HIS-759 AND SER-810.
      Strain: K12.
    10. "Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation."
      Goulding C.W., Matthews R.G.
      Biochemistry 36:15749-15757(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC BINDING SITES.
      Strain: K12.
    11. "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.
    12. "Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy."
      Peariso K., Zhou Z.S., Smith A.E., Matthews R.G., Penner-Hahn J.E.
      Biochemistry 40:987-993(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC BINDING SITES, ROLE OF ZINC IN SUBSTRATE BINDING.
      Strain: K12.
    13. "Cobalamin-dependent methyltransferases."
      Matthews R.G.
      Acc. Chem. Res. 34:681-689(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    14. "How a protein binds B12: a 3.0 A X-ray structure of B12-binding domains of methionine synthase."
      Drennan C.L., Huang S., Drummond J.T., Matthews R.G., Ludwig M.L.
      Science 266:1669-1674(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 651-896 IN COMPLEX WITH COBALAMIN.
    15. "The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12."
      Dixon M.M., Huang S., Matthews R.G., Ludwig M.L.
      Structure 4:1263-1275(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 897-1227 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.
      Strain: K12.
    16. "Domain alternation switches B(12)-dependent methionine synthase to the activation conformation."
      Bandarian V., Pattridge K.A., Lennon B.W., Huddler D.P., Matthews R.G., Ludwig M.L.
      Nat. Struct. Biol. 9:53-56(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 651-1227 OF WILD-TYPE AND MUTANT GLY-759 IN COMPLEX WITH COBALAMIN.
      Strain: K12.

    Entry informationi

    Entry nameiMETH_ECOLI
    AccessioniPrimary (citable) accession number: P13009
    Secondary accession number(s): Q2M6T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    L-homocysteine is bound via the zinc atom.

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3