MMUM_ECOLI
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 03-AUG-2022, entry version 145.
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; Enterobacterales;
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 4.0
RT - 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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=9882684; DOI=10.1128/jb.181.2.662-665.1999;
RA Thanbichler M., Neuhierl B., Boeck A.;
RT "S-methylmethionine metabolism in Escherichia coli.";
RL J. Bacteriol. 181:662-665(1999).
RN [6]
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX 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 methyltransferases.
RT Role in selenium tolerance and evolutionary 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, selenohomocysteine
CC and less efficiently selenocysteine. {ECO:0000269|PubMed:9882684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-
CC methionine; Xref=Rhea:RHEA:26337, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58252; EC=2.1.1.10;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.045 mM for L-homocysteine {ECO:0000269|PubMed:10026151};
CC KM=0.59 mM for L-selenocysteine {ECO:0000269|PubMed:10026151};
CC KM=0.043 mM for DL-selenohomocysteine {ECO:0000269|PubMed:10026151};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10026151}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; NP_414795.1; NC_000913.3.
DR RefSeq; WP_000081352.1; NZ_SSUR01000059.1.
DR RefSeq; YP_001816637.1; NC_010558.1.
DR PDB; 5DML; X-ray; 2.45 A; A=1-310.
DR PDB; 5DMM; X-ray; 1.78 A; A=1-310.
DR PDB; 5DMN; X-ray; 2.89 A; A/B=1-310.
DR PDBsum; 5DML; -.
DR PDBsum; 5DMM; -.
DR PDBsum; 5DMN; -.
DR AlphaFoldDB; Q47690; -.
DR SMR; Q47690; -.
DR BioGRID; 4259777; 8.
DR BioGRID; 850503; 3.
DR IntAct; Q47690; 5.
DR STRING; 511145.b0261; -.
DR jPOST; Q47690; -.
DR PaxDb; Q47690; -.
DR PRIDE; Q47690; -.
DR EnsemblBacteria; AAC73364; AAC73364; b0261.
DR EnsemblBacteria; BAA77929; BAA77929; BAA77929.
DR GeneID; 946143; -.
DR KEGG; ecj:JW0253; -.
DR KEGG; eco:b0261; -.
DR PATRIC; fig|1411691.4.peg.2020; -.
DR eggNOG; COG2040; Bacteria.
DR HOGENOM; CLU_004914_3_2_6; -.
DR InParanoid; Q47690; -.
DR OMA; HRPRMKA; -.
DR PhylomeDB; Q47690; -.
DR BioCyc; EcoCyc:MMUM-MON; -.
DR BioCyc; MetaCyc:MMUM-MON; -.
DR BRENDA; 2.1.1.10; 2026.
DR BRENDA; 2.1.1.280; 2026.
DR SABIO-RK; Q47690; -.
DR PRO; PR:Q47690; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central.
DR GO; GO:0033477; P:S-methylmethionine metabolic process; IMP:EcoCyc.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 1.
DR SUPFAM; SSF82282; SSF82282; 1.
DR PROSITE; PS50970; HCY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..310
FT /note="Homocysteine S-methyltransferase"
FT /id="PRO_0000114610"
FT DOMAIN 1..310
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5DMN"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5DMM"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:5DML"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 85..109
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:5DMM"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 143..159
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:5DMM"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:5DMM"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:5DMM"
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
