METE_YEAST
ID METE_YEAST Reviewed; 767 AA.
AC P05694; D3DLZ8; P38010; Q02488; Q27JJ8;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase;
DE EC=2.1.1.14;
DE AltName: Full=Cobalamin-independent methionine synthase;
DE AltName: Full=Delta-P8 protein;
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme;
GN Name=MET6; OrderedLocusNames=YER091C;
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 204508 / S288c;
RA Korch C., Mountain H.A., Wenzlau J.M.;
RT "Structure and regulation of MET6, the vitamin B12-independent methionine
RT synthase gene of Saccharomyces cerevisiae.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA McClurg J.C.;
RT "Cloning and characterization of MET6: a cobalamin-independent methionine
RT synthase in Saccharomyces cerevisiae.";
RL Thesis (1995), Medical College of Ohio / Toledo, United States.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UCD939, and UCD940;
RA Linderholm A.L., Bisson L.F.;
RT "Allele diversity among genes of the sulfate reduction pathway in wine
RT strains of Saccharomyces cerevisiae.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-486.
RC STRAIN=YMN27;
RA Ohtake Y., Watanabe K., Tezuka H., Ogata T., Yabuuchi S., Murata K.,
RA Kimura A.;
RT "The expression of the gamma-glutamylcysteine synthetase gene of
RT Escherichia coli B in Saccharomyces cerevisiae.";
RL Agric. Biol. Chem. 52:2753-2762(1988).
RN [7]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483834; DOI=10.1002/yea.320110702;
RA Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P.,
RA Perrot M.;
RT "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a
RT gene-protein index.";
RL Yeast 11:601-613(1995).
RN [8]
RP PROTEIN SEQUENCE OF 693-704.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [9]
RP PROTEIN SEQUENCE OF 123-132; 234-243 AND 692-699.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-706, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-566; SER-629 AND SER-706, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC -!- MISCELLANEOUS: Present with 264000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; U32508; AAB60301.1; -; Genomic_DNA.
DR EMBL; U15099; AAA65711.1; -; Genomic_DNA.
DR EMBL; DQ393811; ABD57965.1; -; Genomic_DNA.
DR EMBL; DQ393812; ABD57966.1; -; Genomic_DNA.
DR EMBL; U18839; AAB64646.1; -; Genomic_DNA.
DR EMBL; X07238; CAA30227.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07752.1; -; Genomic_DNA.
DR PIR; S50594; S50594.
DR RefSeq; NP_011015.3; NM_001178982.3.
DR AlphaFoldDB; P05694; -.
DR SMR; P05694; -.
DR BioGRID; 36836; 169.
DR DIP; DIP-6472N; -.
DR IntAct; P05694; 43.
DR MINT; P05694; -.
DR STRING; 4932.YER091C; -.
DR CarbonylDB; P05694; -.
DR iPTMnet; P05694; -.
DR SWISS-2DPAGE; P05694; -.
DR MaxQB; P05694; -.
DR PaxDb; P05694; -.
DR PRIDE; P05694; -.
DR TopDownProteomics; P05694; -.
DR EnsemblFungi; YER091C_mRNA; YER091C; YER091C.
DR GeneID; 856825; -.
DR KEGG; sce:YER091C; -.
DR SGD; S000000893; MET6.
DR VEuPathDB; FungiDB:YER091C; -.
DR eggNOG; KOG2263; Eukaryota.
DR HOGENOM; CLU_013175_0_0_1; -.
DR InParanoid; P05694; -.
DR OMA; KVMKGML; -.
DR BioCyc; MetaCyc:YER091C-MON; -.
DR BioCyc; YEAST:YER091C-MON; -.
DR BRENDA; 2.1.1.14; 984.
DR UniPathway; UPA00051; UER00082.
DR PRO; PR:P05694; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P05694; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR HAMAP; MF_00172; Meth_synth; 1.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Direct protein sequencing; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Phosphoprotein;
KW Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7483834"
FT CHAIN 2..767
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098704"
FT ACT_SITE 705
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 126
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 444..446
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 444..446
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 497
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 497
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 502
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 525
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 528..529
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 574
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 612
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 612
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 737
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 566
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 72..80
FT /note="LSLLFNVIP -> FVFVVQCHS (in Ref. 6; CAA30227)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="A -> R (in Ref. 2; AAA65711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 85860 MW; A553C9A98D35541D CRC64;
MVQSAVLGFP RIGPNRELKK ATEGYWNGKI TVDELFKVGK DLRTQNWKLQ KEAGVDIIPS
NDFSFYDQVL DLSLLFNVIP DRYTKYDLSP IDTLFAMGRG LQRKATETEK AVDVTALEMV
KWFDSNYHYV RPTFSKTTQF KLNGQKPVDE FLEAKELGIH TRPVLLGPVS YLFLGKADKD
SLDLEPLSLL EQLLPLYTEI LSKLASAGAT EVQIDEPVLV LDLPANAQAA IKKAYTYFGE
QSNLPKITLA TYFGTVVPNL DAIKGLPVAA LHVDFVRAPE QFDEVVAAIG NKQTLSVGIV
DGRNIWKNDF KKSSAIVNKA IEKLGADRVV VATSSSLLHT PVDLNNETKL DAEIKGFFSF
ATQKLDEVVV ITKNVSGQDV AAALEANAKS VESRGKSKFI HDAAVKARVA SIDEKMSTRA
APFEQRLPEQ QKVFNLPLFP TTTIGSFPQT KDIRINRNKF NKGTISAEEY EKFINSEIEK
VIRFQEEIGL DVLVHGEPER NDMVQYFGEQ INGYAFTVNG WVQSYGSRYV RPPIIVGDLS
RPKAMSVKES VYAQSITSKP VKGMLTGPIT CLRWSFPRDD VDQKTQAMQL ALALRDEVND
LEAAGIKVIQ VDEPALREGL PLREGTERSA YYTWAAEAFR VATSGVANKT QIHSHFCYSD
LDPNHIKALD ADVVSIEFSK KDDANYIAEF KNYPNHIGLG LFDIHSPRIP SKDEFIAKIS
TILKSYPAEK FWVNPDCGLK TRGWEETRLS LTHMVEAAKY FREQYKN
