Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q49775

- METH_MYCLE

UniProt

Q49775 - METH_MYCLE

Protein

Methionine synthase

Gene

metH

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (27 Apr 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi233 – 2331ZincPROSITE-ProRule annotation
    Metal bindingi299 – 2991ZincPROSITE-ProRule annotation
    Metal bindingi300 – 3001ZincPROSITE-ProRule annotation
    Metal bindingi753 – 7531Cobalt (cobalamin axial ligand)By similarity
    Binding sitei798 – 7981CobalaminBy similarity
    Binding sitei954 – 9541S-adenosyl-L-methionineBy similarity
    Binding sitei1149 – 11491S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1153 – 11531Cobalamin; 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:
    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:ML1307
    ORF Names:B2126_C1_157, MLCB2533.04
    OrganismiMycobacterium leprae (strain TN)
    Taxonomic identifieri272631 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML1307.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12061206Methionine synthasePRO_0000204533Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272631.ML1307.

    Structurei

    3D structure databases

    ProteinModelPortaliQ49775.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 314314Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini350 – 609260Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini642 – 73594B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini740 – 877138B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini907 – 1206300AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni830 – 8312Cobalamin-bindingBy similarity
    Regioni1203 – 12042S-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.

    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.

    Q49775-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVTAANQHQ YDTDLLETLA QRVMVGDGAM GTQLQDAELT LDDFRGLEGC     50
    NEILNETRPD VLETIHRRYF EAGADLVETN TFGCNLSNLG DYDIADKIRD 100
    LSQRGTVIAR RVADELTTPD HKRYVLGSMG PGTKLPTLGH TEYRVVRDAY 150
    TESALGMLDG GADAVLVETC QDLLQLKAAV LGSRRAMTQA GRHIPVFVHV 200
    TVETTGTMLL GSEIGAALAA VEPLGVDMIG LNCATGPAEM SEHLRHLSKH 250
    ARIPVSVMPN AGLPVLGAKG AEYPLQPDEL AEALAGFIAE FGLSLVGGCC 300
    GTTPDHIREV AAAVARCNDG TVPRGERHVT YEPSVSSLYT AIPFAQKPSV 350
    LMIGERTNAN GSKVFREAMI AEDYQKCLDI AKDQTRGGAH LLDLCVDYVG 400
    RNGVADMKAL AGRLATVSTL PIMLDSTEIP VLQAGLEHLG GRCVINSVNY 450
    EDGDGPESRF VKTMELVAEH GAAVVALTID EQGQARTVEK KVEVAERLIN 500
    DITSNWGVDK SAILIDCLTF TIATGQEESR KDGIETIDAI RELKKRHPAV 550
    QTTLGLSNIS FGLNPSARQV LNSVFLHECQ EAGLDSAIVH ASKILPINRI 600
    PEEQRQAALD LVYDRRREGY DPLQKLMWLF KGVSSPSSKE TREAELAKLP 650
    LFDRLAQRIV DGERNGLDVD LDEAMTQKPP LAIINENLLD GMKTVGELFG 700
    SGQMQLPFVL QSAEVMKAAV AYLEPHMEKS DCDFGKGLAK GRIVLATVKG 750
    DVHDIGKNLV DIILSNNGYE VVNLGIKQPI TNILEVAEDK SADVVGMSGL 800
    LVKSTVIMKE NLEEMNTRGV AEKFPVLLGG AALTRSYVEN DLAEVYEGEV 850
    HYARDAFEGL KLMDTIMSAK RGEALAPGSP ESLAAEADRN KETERKARHE 900
    RSKRIAVQRK AAEEPVEVPE RSDVPSDVEV PAPPFWGSRI IKGLAVADYT 950
    GFLDERALFL GQWGLRGVRG GAGPSYEDLV QTEGRPRLRY WLDRLSTYGV 1000
    LAYAAVVYGY FPAVSEDNDI VVLAEPRPDA EQRYRFTFPR QQRGRFLCIA 1050
    DFIRSRDLAT ERSEVDVLPF QLVTMGQPIA DFVGELFVSN SYRDYLEVHG 1100
    IGVQLTEALA EYWHRRIREE LKFSGNRTMS ADDPEAVEDY FKLGYRGARF 1150
    AFGYGACPDL EDRIKMMELL QPERIGVTIS EELQLHPEQS TDAFVLHHPA 1200
    AKYFNV 1206
    Length:1,206
    Mass (Da):132,392
    Last modified:April 27, 2001 - v3
    Checksum:i7786CE5307D7CA86
    GO

    Sequence cautioni

    The sequence AAA17182.1 differs from that shown. Reason: Frameshift at position 873.
    The sequence CAA22918.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00017 Genomic DNA. Translation: AAA17182.1. Frameshift.
    AL035310 Genomic DNA. Translation: CAA22918.1. Different initiation.
    AL583921 Genomic DNA. Translation: CAC31688.1.
    PIRiE87072.
    S72842.
    RefSeqiNP_301940.1. NC_002677.1.
    WP_010908261.1. NC_002677.1.

    Genome annotation databases

    EnsemblBacteriaiCAC31688; CAC31688; CAC31688.
    GeneIDi910429.
    KEGGimle:ML1307.
    PATRICi18054948. VBIMycLep78757_2411.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00017 Genomic DNA. Translation: AAA17182.1 . Frameshift.
    AL035310 Genomic DNA. Translation: CAA22918.1 . Different initiation.
    AL583921 Genomic DNA. Translation: CAC31688.1 .
    PIRi E87072.
    S72842.
    RefSeqi NP_301940.1. NC_002677.1.
    WP_010908261.1. NC_002677.1.

    3D structure databases

    ProteinModelPortali Q49775.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML1307.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC31688 ; CAC31688 ; CAC31688 .
    GeneIDi 910429.
    KEGGi mle:ML1307.
    PATRICi 18054948. VBIMycLep78757_2411.

    Organism-specific databases

    Lepromai ML1307.

    Phylogenomic databases

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

    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. Smith D.R., Robison K.
      Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TN.

    Entry informationi

    Entry nameiMETH_MYCLE
    AccessioniPrimary (citable) accession number: Q49775
    Secondary accession number(s): Q9CC37, Q9S378
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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

    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