ID   MHT1_YEAST              Reviewed;         324 AA.
AC   Q12525;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Homocysteine S-methyltransferase 1;
DE            EC=2.1.1.10;
DE   AltName: Full=S-methylmethionine:homocysteine methyltransferase 1;
DE            Short=SMM:Hcy S-methyltransferase 1;
GN   Name=MHT1; OrderedLocusNames=YLL062C; ORFNames=L0552;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RA   Wedler H., Wambutt R.;
RT   "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces
RT   cerevisiae including the subtelomeric region of the left arm.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=11013242; DOI=10.1074/jbc.M005967200;
RA   Thomas D., Becker A., Surdin-Kerjan Y.;
RT   "Reverse methionine biosynthesis from S-adenosylmethionine in
RT   eukaryotic cells.";
RL   J. Biol. Chem. 275:40718-40724(2000).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Homocysteine S-methyltransferase involved in the
CC       conversion of S-adenosylmethionine (AdoMet) to methionine to
CC       control the methionine/AdoMet ratio. Converts also S-
CC       methylmethionine (SMM) to methionine.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-homocysteine = S-
CC       adenosyl-L-homocysteine + L-methionine.
CC   -!- COFACTOR: Zinc (Potential).
CC   -!- INTERACTION:
CC       Q12043:TGL5; NbExp=1; IntAct=EBI-37133, EBI-34845;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain.
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DR   EMBL; Z47973; CAA87995.1; -; Genomic_DNA.
DR   EMBL; Z73167; CAA97515.1; -; Genomic_DNA.
DR   EMBL; AY558194; AAS56520.1; -; Genomic_DNA.
DR   PIR; S50958; S50958.
DR   RefSeq; NP_013038.1; -.
DR   HSSP; Q93088; 1LT8.
DR   DIP; DIP:1934N; -.
DR   IntAct; Q12525; 5.
DR   Ensembl; YLL062C; Saccharomyces cerevisiae.
DR   GeneID; 850664; -.
DR   GenomeReviews; Y13138_GR; YLL062C.
DR   KEGG; sce:YLL062C; -.
DR   NMPDR; fig|4932.3.peg.4029; -.
DR   CYGD; YLL062c; -.
DR   SGD; S000003985; MHT1.
DR   HOGENOM; Q12525; -.
DR   OMA; Q12525; IRAIYRT.
DR   BRENDA; 2.1.1.10; 250.
DR   NextBio; 966638; -.
DR   ArrayExpress; Q12525; -.
DR   GermOnline; YLL062C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0008898; F:homocysteine S-methyltransferase activity; IDA:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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; Cytoplasm; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN         1    324       Homocysteine S-methyltransferase 1.
FT                                /FTId=PRO_0000114618.
FT   DOMAIN        6    320       Hcy-binding.
FT   METAL       238    238       Zinc (Potential).
FT   METAL       305    305       Zinc (Potential).
FT   METAL       306    306       Zinc (Potential).
SQ   SEQUENCE   324 AA;  36715 MW;  A77194694B6E5C14 CRC64;
     MKRIPIKELI VEHPGKVLIL DGGQGTELEN RGININSPVW SAAPFTSESF WEPSSQERKV
     VEEMYRDFMI AGANILMTIT YQANFQSISE NTSIKTLAAY KRFLDKIVSF TREFIGEERY
     LIGSIGPWAA HVSCEYTGDY GPHPENIDYY GFFKPQLENF NQNRDIDLIG FETIPNFHEL
     KAILSWDEDI ISKPFYIGLS VDDNSLLRDG TTLEEISVHI KGLGNKINKN LLLMGVNCVS
     FNQSALILKM LHEHLPGMPL LVYPNSGEIY NPKEKTWHRP TNKLDDWETT VKKFVDNGAR
     IIGGCCRTSP KDIAEIASAV DKYS
//