MHT1_YEAST
ID MHT1_YEAST Reviewed; 324 AA.
AC Q12525; D6VXU7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
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 (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 [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 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 eukaryotic
RT cells.";
RL J. Biol. Chem. 275:40718-40724(2000).
RN [6]
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 [7]
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).
CC -!- FUNCTION: Homocysteine S-methyltransferase involved in the conversion
CC of S-adenosylmethionine (AdoMet) to methionine to control the
CC methionine/AdoMet ratio. Also converts 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}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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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 EMBL; BK006945; DAA09263.1; -; Genomic_DNA.
DR PIR; S50958; S50958.
DR RefSeq; NP_013038.1; NM_001181882.1.
DR AlphaFoldDB; Q12525; -.
DR SMR; Q12525; -.
DR BioGRID; 31254; 21.
DR DIP; DIP-1934N; -.
DR IntAct; Q12525; 4.
DR MINT; Q12525; -.
DR STRING; 4932.YLL062C; -.
DR MaxQB; Q12525; -.
DR PaxDb; Q12525; -.
DR PRIDE; Q12525; -.
DR EnsemblFungi; YLL062C_mRNA; YLL062C; YLL062C.
DR GeneID; 850664; -.
DR KEGG; sce:YLL062C; -.
DR SGD; S000003985; MHT1.
DR VEuPathDB; FungiDB:YLL062C; -.
DR eggNOG; KOG1579; Eukaryota.
DR GeneTree; ENSGT00510000049619; -.
DR HOGENOM; CLU_004914_3_2_1; -.
DR InParanoid; Q12525; -.
DR OMA; TAVINTH; -.
DR BioCyc; YEAST:YLL062C-MON; -.
DR PRO; PR:Q12525; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12525; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:SGD.
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 Amino-acid biosynthesis; Cytoplasm; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc.
FT CHAIN 1..324
FT /note="Homocysteine S-methyltransferase 1"
FT /id="PRO_0000114618"
FT DOMAIN 6..320
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 305
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"
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
