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Q09582

- METH_CAEEL

UniProt

Q09582 - METH_CAEEL

Protein

Probable methionine synthase

Gene

metr-1

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi249 – 2491ZincPROSITE-ProRule annotation
    Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
    Metal bindingi313 – 3131ZincPROSITE-ProRule annotation
    Metal bindingi775 – 7751Cobalt (cobalamin axial ligand)By similarity
    Binding sitei820 – 8201CobalaminBy similarity
    Binding sitei963 – 9631S-adenosyl-L-methionineBy similarity
    Binding sitei1157 – 11571S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1161 – 11611Cobalamin; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. methionine synthase activity Source: UniProtKB-EC
    3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
    4. zinc ion binding Source: InterPro

    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

    ReactomeiREACT_183520. Sulfur amino acid metabolism.
    REACT_184618. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    REACT_184623. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    REACT_184630. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    UniPathwayiUPA00051; UER00081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable methionine synthase (EC:2.1.1.13)
    Alternative name(s):
    5-methyltetrahydrofolate--homocysteine methyltransferase
    Vitamin-B12 dependent methionine synthase
    Short name:
    MS
    Gene namesi
    Name:metr-1
    ORF Names:R03D7.1
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome II

    Organism-specific databases

    WormBaseiR03D7.1; CE01609; WBGene00010988; metr-1.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12491249Probable methionine synthasePRO_0000204531Add
    BLAST

    Proteomic databases

    PaxDbiQ09582.
    PRIDEiQ09582.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Y76A2B.5Q9XWC91EBI-331777,EBI-331773

    Protein-protein interaction databases

    BioGridi39991. 1 interaction.
    DIPiDIP-26122N.
    IntActiQ09582. 1 interaction.
    MINTiMINT-1116270.
    STRINGi6239.R03D7.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ09582.
    SMRiQ09582. Positions 5-640, 655-1249.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 327327Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini360 – 621262Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini652 – 74998B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini762 – 897136B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini913 – 1249337AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni850 – 8512Cobalamin-bindingBy similarity
    Regioni1211 – 12122S-adenosyl-L-methionine bindingBy similarity

    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 By similarity.By similarity

    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.
    GeneTreeiENSGT00420000029824.
    HOGENOMiHOG000251409.
    InParanoidiQ09582.
    KOiK00548.
    OMAiXAEKDSA.
    OrthoDBiEOG7TF786.
    PhylomeDBiQ09582.

    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.

    Q09582-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRSSLFEEL AEIAKERIMI IDGAMGTMIQ REYMEEEDFR GEILKDHDKP     50
    LKGNNDLLSI TRPDIIYKIH KLYLEAGADF VETNTFSGTT IAQADYRCEH 100
    LVHEINYQSA LVARRACDDV GAATGRRRYV CGAIGPTNRT LSISPSVEKP 150
    DFRNVTFQEL VKAYGDQARS LIQGGVDVLL VETVFDSANA KAALFAIRTL 200
    FEDEGVPEMP VFLSGTIVDM SGRTLSGQTG EAFLVSTKQG KPMAVGLNCA 250
    LGAKDMRQFV DNMSKWSDSF IICYPNAGLP NALGGYDETP EEMADVLREF 300
    ARDGLVNIIG GCCGTTPDHI NAMYKAVQGI TPRVPPQDPH AGKMLLSGLE 350
    PSIVGPETNF VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ 400
    ILDVNMDDGL LDGPYAMSKF LRLISSEPDV AKIPVCIDSS DFDVIIAGLE 450
    STQGKCVVNS ISLKEGEEKF KERARIIKRY GAAVVVMAFD EQGQAAETDP 500
    KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMEEHS NYGMYFIEAA 550
    RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI 600
    VNAGALPVYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD 650
    TKTDEWRSLT VEERLKFALV KGVDQFVVAD TEEARQNTAK YPRPLNVIER 700
    PLMDGMAVVG ELFGAGKMFL PQVIKSARVM KKAVAHLLPF MEIERQANIE 750
    TMGLAEDESP YQGTVVIATV KGDVHDIGKN IVSVVLGCNN FKVVDLGVMT 800
    PCENIIKAAI EEKADFIGLS GLITPSLDEM VYVAKEMNRV GLNIPLLIGG 850
    ATTSKTHTAV KISPRYPHPV VHCLDASKSV VVCSSLSDMS VRDAFLQDLN 900
    EDYEDVRQEH YASLKDRRFT DLNKTREKKF KIDWDKFTAV KPSFVGRREY 950
    QNFDLNELIP YIDWKPFFDV WQLRGKYPNR SYPKIFDDAD VGAEAKKVFD 1000
    DAQTWLKKLI DEKILVANAV VSFLPAASEG DDMHVYDPET GNKLDTFYGL 1050
    RQQSGREHDQ PHFCLSDFIK PLKNGVPDDY LGLFACTAGL GAEEYCKTLE 1100
    KNHDDYASIM VKALADRLAE AYAEYLHKEV RTTLWGYSTN EDLTESDLLS 1150
    IKYQGIRPAC GYPSQPDHTE KRTLWKLLEA EKNGIGLTEH LAMLPAASVS 1200
    GLYFANPQSE YFAVGKIDQD QVIDYAARKN VPKEEVERWL SPILGYDTD 1249
    Length:1,249
    Mass (Da):138,899
    Last modified:November 1, 1996 - v1
    Checksum:i4D16028AD02CD550
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46828 Genomic DNA. Translation: CAA86855.1.
    PIRiT23868.
    RefSeqiNP_496353.1. NM_063952.4.
    UniGeneiCel.16853.

    Genome annotation databases

    EnsemblMetazoaiR03D7.1; R03D7.1; WBGene00010988.
    GeneIDi174681.
    KEGGicel:CELE_R03D7.1.
    UCSCiR03D7.1. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46828 Genomic DNA. Translation: CAA86855.1 .
    PIRi T23868.
    RefSeqi NP_496353.1. NM_063952.4.
    UniGenei Cel.16853.

    3D structure databases

    ProteinModelPortali Q09582.
    SMRi Q09582. Positions 5-640, 655-1249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 39991. 1 interaction.
    DIPi DIP-26122N.
    IntActi Q09582. 1 interaction.
    MINTi MINT-1116270.
    STRINGi 6239.R03D7.1.

    Proteomic databases

    PaxDbi Q09582.
    PRIDEi Q09582.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai R03D7.1 ; R03D7.1 ; WBGene00010988 .
    GeneIDi 174681.
    KEGGi cel:CELE_R03D7.1.
    UCSCi R03D7.1. c. elegans.

    Organism-specific databases

    CTDi 174681.
    WormBasei R03D7.1 ; CE01609 ; WBGene00010988 ; metr-1.

    Phylogenomic databases

    eggNOGi COG1410.
    GeneTreei ENSGT00420000029824.
    HOGENOMi HOG000251409.
    InParanoidi Q09582.
    KOi K00548.
    OMAi XAEKDSA.
    OrthoDBi EOG7TF786.
    PhylomeDBi Q09582.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .
    Reactomei REACT_183520. Sulfur amino acid metabolism.
    REACT_184618. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    REACT_184623. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    REACT_184630. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Miscellaneous databases

    NextBioi 885042.
    PROi Q09582.

    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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.

    Entry informationi

    Entry nameiMETH_CAEEL
    AccessioniPrimary (citable) accession number: Q09582
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Miscellaneous

    L-homocysteine is bound via the zinc atom.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3