SAM4_YEAST
ID SAM4_YEAST Reviewed; 325 AA.
AC Q08985; D6W397;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Homocysteine S-methyltransferase 2;
DE EC=2.1.1.10;
DE AltName: Full=S-adenosylmethionine metabolism protein 4;
DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 2;
DE Short=SMM:Hcy S-methyltransferase 2;
GN Name=SAM4; OrderedLocusNames=YPL273W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX 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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
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 eukaryotic
RT cells.";
RL J. Biol. Chem. 275:40718-40724(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX 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 [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Homocysteine S-methyltransferase involved in the conversion
CC of S-adenosylmethionine (AdoMet) to methionine to control the
CC methionine/AdoMet ratio. Converts also S-methylmethionine (SMM) to
CC methionine. {ECO:0000269|PubMed:11013242}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Up-regulated in response to high extracellular methionine.
CC {ECO:0000269|PubMed:11013242}.
CC -!- MISCELLANEOUS: Present with 60300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73629; CAA98009.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11163.1; -; Genomic_DNA.
DR PIR; S65306; S65306.
DR RefSeq; NP_015050.1; NM_001184087.1.
DR AlphaFoldDB; Q08985; -.
DR SMR; Q08985; -.
DR BioGRID; 35940; 35.
DR STRING; 4932.YPL273W; -.
DR iPTMnet; Q08985; -.
DR MaxQB; Q08985; -.
DR PaxDb; Q08985; -.
DR PRIDE; Q08985; -.
DR DNASU; 855855; -.
DR EnsemblFungi; YPL273W_mRNA; YPL273W; YPL273W.
DR GeneID; 855855; -.
DR KEGG; sce:YPL273W; -.
DR SGD; S000006194; SAM4.
DR VEuPathDB; FungiDB:YPL273W; -.
DR eggNOG; KOG1579; Eukaryota.
DR GeneTree; ENSGT00510000049619; -.
DR HOGENOM; CLU_004914_3_2_1; -.
DR InParanoid; Q08985; -.
DR OMA; HRPRMKA; -.
DR BioCyc; YEAST:YPL273W-MON; -.
DR PRO; PR:Q08985; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08985; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:SGD.
DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
DR GO; GO:0050667; P:homocysteine metabolic process; IDA:SGD.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IDA:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; IDA:SGD.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SUPFAM; SSF82282; SSF82282; 1.
DR PROSITE; PS50970; HCY; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..325
FT /note="Homocysteine S-methyltransferase 2"
FT /id="PRO_0000114619"
FT DOMAIN 6..321
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
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
