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Protein

Homocysteine S-methyltransferase

Gene

mmuM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes methyl transfer from S-methylmethionine or S-adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine.1 Publication

Catalytic activityi

S-methyl-L-methionine + L-homocysteine = 2 L-methionine.

Cofactori

Zn2+PROSITE-ProRule annotation

Kineticsi

  1. KM=0.045 mM for L-homocysteine1 Publication
  2. KM=0.59 mM for L-selenocysteine1 Publication
  3. KM=0.043 mM for DL-selenohomocysteine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi229 – 2291ZincPROSITE-ProRule annotation
    Metal bindingi295 – 2951ZincPROSITE-ProRule annotation
    Metal bindingi296 – 2961ZincPROSITE-ProRule annotation

    GO - Molecular functioni

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: EcoliWiki
    • methionine biosynthetic process Source: UniProtKB-KW
    • S-methylmethionine metabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:MMUM-MONOMER.
    ECOL316407:JW0253-MONOMER.
    MetaCyc:MMUM-MONOMER.
    BRENDAi2.1.1.10. 2026.
    2.1.1.280. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homocysteine S-methyltransferase (EC:2.1.1.10)
    Alternative name(s):
    S-methylmethionine:homocysteine methyltransferase
    Gene namesi
    Name:mmuM
    Synonyms:yagD
    Ordered Locus Names:b0261, JW0253
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13343. mmuM.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 310310Homocysteine S-methyltransferasePRO_0000114610Add
    BLAST

    Proteomic databases

    PaxDbiQ47690.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4259777. 8 interactions.
    IntActiQ47690. 5 interactions.
    STRINGi511145.b0261.

    Structurei

    Secondary structure

    1
    310
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Beta strandi17 – 193Combined sources
    Helixi24 – 296Combined sources
    Helixi39 – 468Combined sources
    Helixi48 – 6114Combined sources
    Beta strandi64 – 674Combined sources
    Turni69 – 724Combined sources
    Helixi75 – 784Combined sources
    Helixi79 – 813Combined sources
    Helixi85 – 10925Combined sources
    Helixi111 – 1133Combined sources
    Beta strandi117 – 1226Combined sources
    Helixi125 – 1295Combined sources
    Turni133 – 1364Combined sources
    Helixi143 – 15917Combined sources
    Beta strandi163 – 1708Combined sources
    Helixi173 – 18311Combined sources
    Beta strandi191 – 1955Combined sources
    Beta strandi197 – 1993Combined sources
    Helixi209 – 2179Combined sources
    Beta strandi222 – 2298Combined sources
    Helixi232 – 2343Combined sources
    Helixi235 – 2439Combined sources
    Beta strandi250 – 2534Combined sources
    Helixi277 – 2804Combined sources
    Helixi281 – 2866Combined sources
    Beta strandi289 – 2924Combined sources
    Helixi300 – 30910Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5DMLX-ray2.45A1-310[»]
    5DMMX-ray1.78A1-310[»]
    5DMNX-ray2.89A/B1-310[»]
    ProteinModelPortaliQ47690.
    SMRiQ47690. Positions 11-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 310310Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Hcy-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4107QK5. Bacteria.
    COG2040. LUCA.
    HOGENOMiHOG000265278.
    InParanoidiQ47690.
    KOiK00547.
    OMAiWISFSAK.
    OrthoDBiEOG6C019S.
    PhylomeDBiQ47690.

    Family and domain databases

    Gene3Di3.20.20.330. 1 hit.
    InterProiIPR003726. HCY_dom.
    [Graphical view]
    PfamiPF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    SUPFAMiSSF82282. SSF82282. 1 hit.
    PROSITEiPS50970. HCY. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q47690-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQNNPLRAL LDKQDILLLD GAMATELEAR GCNLADSLWS AKVLVENPEL
    60 70 80 90 100
    IREVHLDYYR AGAQCAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR
    110 120 130 140 150
    KAREAYLAEN PQAGTLLVAG SVGPYGAYLA DGSEYRGDYH CSVEAFQAFH
    160 170 180 190 200
    RPRVEALLDA GADLLACETL PNFSEIEALA ELLTAYPRAR AWFSFTLRDS
    210 220 230 240 250
    EHLSDGTPLR DVVALLAGYP QVVALGINCI ALENTTAALQ HLHGLTVLPL
    260 270 280 290 300
    VVYPNSGEHY DAVSKTWHHH GEHCAQLADY LPQWQAAGAR LIGGCCRTTP
    310
    ADIAALKARS
    Length:310
    Mass (Da):33,423
    Last modified:November 1, 1997 - v2
    Checksum:i8381CFF475E5FB7A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U70214 Genomic DNA. Translation: AAB08682.1.
    U00096 Genomic DNA. Translation: AAC73364.1.
    AP009048 Genomic DNA. Translation: BAA77929.2.
    PIRiE64751.
    RefSeqiNP_414795.1. NC_000913.3.
    WP_000081352.1. NZ_LN832404.1.
    YP_001816637.1. NC_010558.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73364; AAC73364; b0261.
    BAA77929; BAA77929; BAA77929.
    GeneIDi6275998.
    946143.
    KEGGiecj:JW0253.
    eco:b0261.
    pg:6275998.
    PATRICi32115641. VBIEscCol129921_0264.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U70214 Genomic DNA. Translation: AAB08682.1.
    U00096 Genomic DNA. Translation: AAC73364.1.
    AP009048 Genomic DNA. Translation: BAA77929.2.
    PIRiE64751.
    RefSeqiNP_414795.1. NC_000913.3.
    WP_000081352.1. NZ_LN832404.1.
    YP_001816637.1. NC_010558.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5DMLX-ray2.45A1-310[»]
    5DMMX-ray1.78A1-310[»]
    5DMNX-ray2.89A/B1-310[»]
    ProteinModelPortaliQ47690.
    SMRiQ47690. Positions 11-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259777. 8 interactions.
    IntActiQ47690. 5 interactions.
    STRINGi511145.b0261.

    Proteomic databases

    PaxDbiQ47690.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73364; AAC73364; b0261.
    BAA77929; BAA77929; BAA77929.
    GeneIDi6275998.
    946143.
    KEGGiecj:JW0253.
    eco:b0261.
    pg:6275998.
    PATRICi32115641. VBIEscCol129921_0264.

    Organism-specific databases

    EcoGeneiEG13343. mmuM.

    Phylogenomic databases

    eggNOGiENOG4107QK5. Bacteria.
    COG2040. LUCA.
    HOGENOMiHOG000265278.
    InParanoidiQ47690.
    KOiK00547.
    OMAiWISFSAK.
    OrthoDBiEOG6C019S.
    PhylomeDBiQ47690.

    Enzyme and pathway databases

    BioCyciEcoCyc:MMUM-MONOMER.
    ECOL316407:JW0253-MONOMER.
    MetaCyc:MMUM-MONOMER.
    BRENDAi2.1.1.10. 2026.
    2.1.1.280. 2026.

    Miscellaneous databases

    PROiQ47690.

    Family and domain databases

    Gene3Di3.20.20.330. 1 hit.
    InterProiIPR003726. HCY_dom.
    [Graphical view]
    PfamiPF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    SUPFAMiSSF82282. SSF82282. 1 hit.
    PROSITEiPS50970. HCY. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
      Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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], SEQUENCE REVISION TO 123; 130; 142 AND 159.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "S-methylmethionine metabolism in Escherichia coli."
      Thanbichler M., Neuhierl B., Boeck A.
      J. Bacteriol. 181:662-665(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "A family of S-methylmethionine-dependent thiol/selenol methyltransferases. Role in selenium tolerance and evolutionary relation."
      Neuhierl B., Thanbichler M., Lottspeich F., Boeck A.
      J. Biol. Chem. 274:5407-5414(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: K12 / JM109 / ATCC 53323.

    Entry informationi

    Entry nameiMMUM_ECOLI
    AccessioniPrimary (citable) accession number: Q47690
    Secondary accession number(s): P77226
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: March 16, 2016
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.