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A8XY95

- METH_CAEBR

UniProt

A8XY95 - METH_CAEBR

Protein

Probable methionine synthase

Gene

metr-1

Organism
Caenorhabditis briggsae
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      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 sitei977 – 9771S-adenosyl-L-methionineBy similarity
    Binding sitei1171 – 11711S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1175 – 11751Cobalamin; 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

    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:CBG20636
    OrganismiCaenorhabditis briggsae
    Taxonomic identifieri6238 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000008549: Chromosome II, UP000008549: Unassembled WGS sequence

    Organism-specific databases

    WormBaseiCBG20636; CBP26766; WBGene00039583; Cbr-metr-1.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12731273Probable methionine synthasePRO_0000412913Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi6238.CBG20636.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 327321Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini360 – 621262Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini652 – 74998B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini762 – 897136B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini927 – 1273347AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni850 – 8512Cobalamin-bindingBy similarity
    Regioni1225 – 12262S-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.
    HOGENOMiHOG000251409.
    OrthoDBiEOG7TF786.

    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.

    A8XY95-1 [UniParc]FASTAAdd to Basket

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    MTRSSLFKEL ADIAKERIMI IDGAMGTMIQ REYMEEHDFR GEILKDHDKP     50
    LKGNNDLLSI TRPDIIYKIH KLYLEAGADF IETNTFSGTT IAQADYHCEH 100
    LVHEINYQSA LVARRACDDV GAATGIRRYV CGAIGPTNRT LSISPSVEKP 150
    DFRNVTFQEL VKAYGDQARS LIQGGVDVLL VETVFDSANA KAALFAIRTL 200
    FEDEGVPEIP VFLSGTIVDM SGRTLSGQTG EAFLVSTKQG KPIAVGLNCA 250
    LGAKDMRQFV QNMSLWSDTL ILCYPNAGLP NALGGYDETP EEMAEVLREF 300
    AQDGLVNIIG GCCGTTPDHI NAMYKAVQGI SPRVPPADPH AGKMLLSGLE 350
    PSIVGPETNF VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ 400
    ILDVNMDDGL LDGPYAMSKF LRLISSEPDV AKIPVCIDSS DFDVIIAGLE 450
    STQGKCVVNS ISLKEGEEKF KERARIVKRY GAAVVVMAFD EEGQAAETER 500
    KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMDEHA NYGMYFIEAT 550
    RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI 600
    VNAGALPVYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD 650
    TKTDEWRNTS VEERLKFALV KGIDQFVVAD TEEARQNTEK YPRPLNVIER 700
    PLMDGMAVVG ELFGAGKMFL PQVIKSARVM KKAVAHLLPF MDAERQANIE 750
    KMGLDEDESP YQGTVVIATV KGDVHDIGKN IVAVVLGCNN FKVVDLGVMT 800
    PCENIIKAAI EEKADFIGLS GLITPSLDEM VHVAKEMNRV GLKIPLLIGG 850
    ATTSKTHTAV KIAPRYPHPV VHCLDASKSV VVCSSLSDMT VRDAFLQDLN 900
    EDYEDVRTKM CLVSYLNHFF ITEHYESLKD RRFVALGKTR EKKFNIDWNK 950
    FSPVKPSFIG RREFQNFDFK ELIPYIDWKP FFDVWQLRGK YPNRSYPKIF 1000
    DDADVGGEAK RVFDDAQTWL KKLIDEKVLT ANAVVSFLPA ASEGDDIHVY 1050
    DPETGNKLDT FYGLRQQSGR EHDQSHFCLS DFIRPLKIGV PDDYLGLFAC 1100
    TAGLGAEEYC KVLEENHDDY ASIMVKALAD RLAEAYAEYL HKEVRVNLWG 1150
    YSTNEQLTET DLLSIKYEGI RPACGYPSQP DHTEKRTLWK LLEAEKNGIV 1200
    LTEHLAMLPA ASVSGLYFAN PQSQYFAVGK IDEDQVAFIY VRSKNVTDYA 1250
    ARKNVPKEEV ERWLSPIIGY ELD 1273
    Length:1,273
    Mass (Da):141,762
    Last modified:December 16, 2008 - v2
    Checksum:i7178233645CE06AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE600991 Genomic DNA. Translation: CAP37612.2.

    Genome annotation databases

    EnsemblMetazoaiCBG20636; CBG20636; CBG20636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE600991 Genomic DNA. Translation: CAP37612.2 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6238.CBG20636.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai CBG20636 ; CBG20636 ; CBG20636 .

    Organism-specific databases

    WormBasei CBG20636 ; CBP26766 ; WBGene00039583 ; Cbr-metr-1.

    Phylogenomic databases

    eggNOGi COG1410.
    HOGENOMi HOG000251409.
    OrthoDBi EOG7TF786.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AF16.

    Entry informationi

    Entry nameiMETH_CAEBR
    AccessioniPrimary (citable) accession number: A8XY95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 49 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3