ID   MMUM_ECOLI              Reviewed;         310 AA.
AC   Q47690; P77226;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Homocysteine S-methyltransferase;
DE            EC=2.1.1.10;
DE   AltName: Full=S-methylmethionine:homocysteine methyltransferase;
GN   Name=mmuM; Synonyms=yagD; OrderedLocusNames=b0261, JW0253;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA   Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA   Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the
RT   4.0 - 6.0 min (189,987 - 281,416bp) region.";
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
RP   TO 123; 130; 142 AND 159.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=99102233; PubMed=9882684;
RA   Thanbichler M., Neuhierl B., Boeck A.;
RT   "S-methylmethionine metabolism in Escherichia coli.";
RL   J. Bacteriol. 181:662-665(1999).
RN   [6]
RP   CHARACTERIZATION.
RC   STRAIN=K12 / JM109 / ATCC 53323;
RX   MEDLINE=99150319; PubMed=10026151; DOI=10.1074/jbc.274.9.5407;
RA   Neuhierl B., Thanbichler M., Lottspeich F., Boeck A.;
RT   "A family of S-methylmethionine-dependent thiol/selenol
RT   methyltransferases. Role in selenium tolerance and evolutionary
RT   relation.";
RL   J. Biol. Chem. 274:5407-5414(1999).
CC   -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine or S-
CC       adenosylmethionine (less efficient) to homocysteine,
CC       selenohomocysteine and less efficiently selenocysteine.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-homocysteine = S-
CC       adenosyl-L-homocysteine + L-methionine.
CC   -!- COFACTOR: Zinc (Potential).
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain.
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DR   EMBL; U70214; AAB08682.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73364.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA77929.2; -; Genomic_DNA.
DR   PIR; E64751; E64751.
DR   RefSeq; AP_000914.1; -.
DR   RefSeq; NP_414795.1; -.
DR   GeneID; 946143; -.
DR   GenomeReviews; AP009048_GR; JW0253.
DR   GenomeReviews; U00096_GR; b0261.
DR   KEGG; ecj:JW0253; -.
DR   KEGG; eco:b0261; -.
DR   EcoGene; EG13343; mmuM.
DR   HOGENOM; Q47690; -.
DR   OMA; Q47690; NSYALVP.
DR   BioCyc; EcoCyc:MMUM-MON; -.
DR   BioCyc; MetaCyc:MMUM-MON; -.
DR   GO; GO:0008898; F:homocysteine S-methyltransferase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003726; S_MeTrfase.
DR   Gene3D; G3DSA:3.20.20.330; S_methyl_trans; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN         1    310       Homocysteine S-methyltransferase.
FT                                /FTId=PRO_0000114610.
FT   DOMAIN        1    310       Hcy-binding.
FT   METAL       229    229       Zinc (Potential).
FT   METAL       295    295       Zinc (Potential).
FT   METAL       296    296       Zinc (Potential).
SQ   SEQUENCE   310 AA;  33423 MW;  8381CFF475E5FB7A CRC64;
     MSQNNPLRAL LDKQDILLLD GAMATELEAR GCNLADSLWS AKVLVENPEL IREVHLDYYR
     AGAQCAITAS YQATPAGFAA RGLDEAQSKA LIGKSVELAR KAREAYLAEN PQAGTLLVAG
     SVGPYGAYLA DGSEYRGDYH CSVEAFQAFH RPRVEALLDA GADLLACETL PNFSEIEALA
     ELLTAYPRAR AWFSFTLRDS EHLSDGTPLR DVVALLAGYP QVVALGINCI ALENTTAALQ
     HLHGLTVLPL VVYPNSGEHY DAVSKTWHHH GEHCAQLADY LPQWQAAGAR LIGGCCRTTP
     ADIAALKARS
//