ID   SAM4_YEAST              Reviewed;         325 AA.
AC   Q08985;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Homocysteine S-methyltransferase 2;
DE            EC=2.1.1.10;
DE   AltName: Full=S-methylmethionine:homocysteine methyltransferase 2;
DE            Short=SMM:Hcy S-methyltransferase 2;
DE   AltName: Full=S-adenosylmethionine metabolism protein 4;
GN   Name=SAM4; OrderedLocusNames=YPL273W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   FUNCTION, AND INDUCTION.
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   [3]
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   [4]
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND THR-138, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
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   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- INDUCTION: Up-regulated in response to high extracellular
CC       methionine.
CC   -!- MISCELLANEOUS: Present with 60300 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain.
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DR   EMBL; Z73629; CAA98009.1; -; Genomic_DNA.
DR   PIR; S65306; S65306.
DR   RefSeq; NP_015050.1; -.
DR   PeptideAtlas; Q08985; -.
DR   PRIDE; Q08985; -.
DR   Ensembl; YPL273W; Saccharomyces cerevisiae.
DR   GeneID; 855855; -.
DR   GenomeReviews; U00094_GR; YPL273W.
DR   KEGG; sce:YPL273W; -.
DR   NMPDR; fig|4932.3.peg.6174; -.
DR   CYGD; YPL273w; -.
DR   SGD; S000006194; SAM4.
DR   HOGENOM; Q08985; -.
DR   OMA; Q08985; DESSANR.
DR   BRENDA; 2.1.1.10; 250.
DR   NextBio; 980460; -.
DR   GermOnline; YPL273W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0008898; F:homocysteine S-methyltransferase activity; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050667; P:homocysteine metabolic process; IDA:SGD.
DR   GO; GO:0019284; P:methionine biosynthetic process from S-aden...; IDA:SGD.
DR   GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IDA:SGD.
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; Nucleus; Phosphoprotein;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    325       Homocysteine S-methyltransferase 2.
FT                                /FTId=PRO_0000114619.
FT   DOMAIN        6    321       Hcy-binding.
FT   METAL       239    239       Zinc (Potential).
FT   METAL       306    306       Zinc (Potential).
FT   METAL       307    307       Zinc (Potential).
FT   MOD_RES      99     99       Phosphoserine.
FT   MOD_RES     138    138       Phosphothreonine.
SQ   SEQUENCE   325 AA;  36669 MW;  54658C7B92A610F0 CRC64;
     MARLPLKQFL ADNPKKVLVL DGGQGTELEN RGIKVANPVW STIPFISESF WSDESSANRK
     IVKEMFNDFL NAGAEILMTT TYQTSYKSVS ENTPIRTLSE YNNLLNRIVD FSRNCIGEDK
     YLIGCIGPWG AHICREFTGD YGAEPENIDF YQYFKPQLEN FNKNDKLDLI GFETIPNIHE
     LKAILSWDES ILSRPFYIGL SVHEHGVLRD GTTMEEIAQV IKDLGDKINP NFSFLGINCV
     SFNQSPDILE SLHQALPNMA LLAYPNSGEV YDTEKKIWLP NSDKLNSWDT VVKQYISSGA
     RIIGGCCRTS PKDIQEISAA VKKYT
//