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O33259

- METH_MYCTU

UniProt

O33259 - METH_MYCTU

Protein

Methionine synthase

Gene

metH

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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 bindingi231 – 2311ZincPROSITE-ProRule annotation
    Metal bindingi297 – 2971ZincPROSITE-ProRule annotation
    Metal bindingi298 – 2981ZincPROSITE-ProRule annotation
    Metal bindingi742 – 7421Cobalt (cobalamin axial ligand)By similarity
    Binding sitei787 – 7871CobalaminBy similarity
    Binding sitei940 – 9401S-adenosyl-L-methionineBy similarity
    Binding sitei1135 – 11351S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1139 – 11391Cobalamin; 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

    BioCyciMTBRV:RV2124C-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:Rv2124c
    ORF Names:MTCY261.20c
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv2124c.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: MTBBASE
    2. cytosol Source: MTBBASE
    3. plasma membrane Source: MTBBASE

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11921192Methionine synthasePRO_0000204534Add
    BLAST

    Proteomic databases

    PRIDEiO33259.

    Interactioni

    Protein-protein interaction databases

    STRINGi83332.Rv2124c.

    Structurei

    3D structure databases

    ProteinModelPortaliO33259.
    SMRiO33259. Positions 16-621, 637-1192.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 312312Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini343 – 601259Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini635 – 72894B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini729 – 866138B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini893 – 1192300AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni819 – 8202Cobalamin-bindingBy similarity
    Regioni1189 – 11902S-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.
    HOGENOMiHOG000251408.
    KOiK00548.
    OMAiLTEHYAM.
    OrthoDBiEOG6091CH.
    PhylomeDBiO33259.

    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.

    O33259-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAADKHLYD TDLLDVLSQR VMVGDGAMGT QLQAADLTLD DFRGLEGCNE     50
    ILNETRPDVL ETIHRNYFEA GADAVETNTF GCNLSNLGDY DIADRIRDLS 100
    QKGTAIARRV ADELGSPDRK RYVLGSMGPG TKLPTLGHTE YAVIRDAYTE 150
    AALGMLDGGA DAILVETCQD LLQLKAAVLG SRRAMTRAGR HIPVFAHVTV 200
    ETTGTMLLGS EIGAALTAVE PLGVDMIGLN CATGPAEMSE HLRHLSRHAR 250
    IPVSVMPNAG LPVLGAKGAE YPLLPDELAE ALAGFIAEFG LSLVGGCCGT 300
    TPAHIREVAA AVANIKRPER QVSYEPSVSS LYTAIPFAQD ASVLVIGERT 350
    NANGSKGFRE AMIAEDYQKC LDIAKDQTRD GAHLLDLCVD YVGRDGVADM 400
    KALASRLATS STLPIMLDST ETAVLQAGLE HLGGRCAINS VNYEDGDGPE 450
    SRFAKTMALV AEHGAAVVAL TIDEEGQART AQKKVEIAER LINDITGNWG 500
    VDESSILIDT LTFTIATGQE ESRRDGIETI EAIRELKKRH PDVQTTLGLS 550
    NISFGLNPAA RQVLNSVFLH ECQEAGLDSA IVHASKILPM NRIPEEQRNV 600
    ALDLVYDRRR EDYDPLQELM RLFEGVSAAS SKEDRLAELA GLPLFERLAQ 650
    RIVDGERNGL DADLDEAMTQ KPPLQIINEH LLAGMKTVGE LFGSGQMQLP 700
    FVLQSAEVMK AAVAYLEPHM ERSDDDSGKG RIVLATVKGD VHDIGKNLVD 750
    IILSNNGYEV VNIGIKQPIA TILEVAEDKS ADVVGMSGLL VKSTVVMKEN 800
    LEEMNTRGVA EKFPVLLGGA ALTRSYVEND LAEIYQGEVH YARDAFEGLK 850
    LMDTIMSAKR GEAPDENSPE AIKAREKEAE RKARHQRSKR IAAQRKAAEE 900
    PVEVPERSDV AADIEVPAPP FWGSRIVKGL AVADYTGLLD ERALFLGQWG 950
    LRGQRGGEGP SYEDLVETEG RPRLRYWLDR LSTDGILAHA AVVYGYFPAV 1000
    SEGNDIVVLT EPKPDAPVRY RFHFPRQQRG RFLCIADFIR SRELAAERGE 1050
    VDVLPFQLVT MGQPIADFAN ELFASNAYRD YLEVHGIGVQ LTEALAEYWH 1100
    RRIREELKFS GDRAMAAEDP EAKEDYFKLG YRGARFAFGY GACPDLEDRA 1150
    KMMALLEPER IGVTLSEELQ LHPEQSTDAF VLHHPEAKYF NV 1192
    Length:1,192
    Mass (Da):130,323
    Last modified:January 1, 1998 - v1
    Checksum:i820450DCE77BE15B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP44899.1.
    PIRiG70513.
    RefSeqiNP_216640.1. NC_000962.3.
    YP_006515540.1. NC_018143.2.

    Genome annotation databases

    EnsemblBacteriaiCCP44899; CCP44899; Rv2124c.
    GeneIDi13316931.
    888711.
    KEGGimtu:Rv2124c.
    mtv:RVBD_2124c.
    PATRICi18153284. VBIMycTub87468_2371.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP44899.1 .
    PIRi G70513.
    RefSeqi NP_216640.1. NC_000962.3.
    YP_006515540.1. NC_018143.2.

    3D structure databases

    ProteinModelPortali O33259.
    SMRi O33259. Positions 16-621, 637-1192.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 83332.Rv2124c.

    Proteomic databases

    PRIDEi O33259.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCP44899 ; CCP44899 ; Rv2124c .
    GeneIDi 13316931.
    888711.
    KEGGi mtu:Rv2124c.
    mtv:RVBD_2124c.
    PATRICi 18153284. VBIMycTub87468_2371.

    Organism-specific databases

    TubercuListi Rv2124c.

    Phylogenomic databases

    eggNOGi COG1410.
    HOGENOMi HOG000251408.
    KOi K00548.
    OMAi LTEHYAM.
    OrthoDBi EOG6091CH.
    PhylomeDBi O33259.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .
    BioCyci MTBRV:RV2124C-MONOMER.

    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: ATCC 25618 / H37Rv.
    2. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
      Raman K., Yeturu K., Chandra N.
      BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.

    Entry informationi

    Entry nameiMETH_MYCTU
    AccessioniPrimary (citable) accession number: O33259
    Secondary accession number(s): L0T8Q3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 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.By similarity
    Was identified as a high-confidence drug target.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3