MTAP_YEAST
ID MTAP_YEAST Reviewed; 337 AA.
AC Q07938; D6VY19; E9P915; Q06899;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE EC=2.4.2.28 {ECO:0000255|HAMAP-Rule:MF_03155};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTAPase {ECO:0000255|HAMAP-Rule:MF_03155};
DE AltName: Full=Multicopy enhancer of UAS2;
GN Name=MEU1 {ECO:0000255|HAMAP-Rule:MF_03155}; OrderedLocusNames=YLR017W;
GN ORFNames=L1595;
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 Saville S.P., Atkinson S., Jamieson L., Pocklington M.J., Orr E.;
RT "A 7.8kb fragment from chromosome XII of Saccharomyces cerevisiae does not
RT harbour PKC2.";
RL Submitted (SEP-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, AND SUBCELLULAR LOCATION.
RX PubMed=8807288; DOI=10.1093/genetics/143.3.1137;
RA Donoviel M.S., Young E.T.;
RT "Isolation and identification of genes activating UAS2-dependent ADH2
RT expression in Saccharomyces cerevisiae.";
RL Genetics 143:1137-1148(1996).
RN [6]
RP FUNCTION.
RX PubMed=14506228; DOI=10.1074/jbc.m308451200;
RA Subhi A.L., Diegelman P., Porter C.W., Tang B., Lu Z.J., Markham G.D.,
RA Kruger W.D.;
RT "Methylthioadenosine phosphorylase regulates ornithine decarboxylase by
RT production of downstream metabolites.";
RL J. Biol. Chem. 278:49868-49873(2003).
RN [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=16530730; DOI=10.1016/j.bbrc.2006.02.144;
RA Chattopadhyay M.K., Tabor C.W., Tabor H.;
RT "Methylthioadenosine and polyamine biosynthesis in a Saccharomyces
RT cerevisiae meu1delta mutant.";
RL Biochem. Biophys. Res. Commun. 343:203-207(2006).
RN [10]
RP FUNCTION.
RX PubMed=18625006; DOI=10.1111/j.1742-4658.2008.06552.x;
RA Pirkov I., Norbeck J., Gustafsson L., Albers E.;
RT "A complete inventory of all enzymes in the eukaryotic methionine salvage
RT pathway.";
RL FEBS J. 275:4111-4120(2008).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.
CC Involved in the breakdown of MTA, a major by-product of polyamine
CC biosynthesis. Responsible for the first step in the methionine salvage
CC pathway after MTA has been generated from S-adenosylmethionine. Has
CC broad substrate specificity with 6-aminopurine nucleosides as preferred
CC substrates. Seems to be implicated in the regulation of the expression
CC of the ADH2 gene. {ECO:0000255|HAMAP-Rule:MF_03155,
CC ECO:0000269|PubMed:14506228, ECO:0000269|PubMed:16530730,
CC ECO:0000269|PubMed:18625006, ECO:0000269|PubMed:8807288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03155};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (phosphorylase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03155}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 4820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03155}.
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DR EMBL; X90564; CAA62156.1; -; Genomic_DNA.
DR EMBL; Z73189; CAA97539.1; -; Genomic_DNA.
DR EMBL; AY693070; AAT93089.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09335.1; -; Genomic_DNA.
DR PIR; S64839; S64839.
DR RefSeq; NP_013117.1; NM_001181904.1.
DR AlphaFoldDB; Q07938; -.
DR SMR; Q07938; -.
DR BioGRID; 31291; 87.
DR DIP; DIP-989N; -.
DR IntAct; Q07938; 2.
DR STRING; 4932.YLR017W; -.
DR iPTMnet; Q07938; -.
DR MaxQB; Q07938; -.
DR PaxDb; Q07938; -.
DR PRIDE; Q07938; -.
DR EnsemblFungi; YLR017W_mRNA; YLR017W; YLR017W.
DR GeneID; 850704; -.
DR KEGG; sce:YLR017W; -.
DR SGD; S000004007; MEU1.
DR VEuPathDB; FungiDB:YLR017W; -.
DR eggNOG; KOG3985; Eukaryota.
DR GeneTree; ENSGT00950000182991; -.
DR HOGENOM; CLU_054456_0_1_1; -.
DR OMA; ADPFCPE; -.
DR BioCyc; YEAST:MON3O-157; -.
DR Reactome; R-SCE-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00873.
DR PRO; PR:Q07938; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07938; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IDA:SGD.
DR GO; GO:0006537; P:glutamate biosynthetic process; IMP:SGD.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:SGD.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..337
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000184556"
FT BINDING 41
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 88..89
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 121..122
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 231
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 254..256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT SITE 212
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT SITE 267
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT CONFLICT 55
FT /note="L -> V (in Ref. 1; CAA62156)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> G (in Ref. 4; AAT93089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37857 MW; 99B54F62ED8A9389 CRC64;
MNRIKNTFSV AKRLKLSKVM TNSELPSIFE GTVDLGIIGG TGLYNLDCLE PIALLPPMVT
PWGTTSSPVT ISQFVGTNSH FHVAFIARHG INHEYPPTKV PFRANMAALK NLNCKAVLSF
SAVGSLQPHI KPRDFVLPQQ IIDRTKGIRH SSYFNDEGLV GHVGFGQPFS QKFAEYIYQF
KNEITNPESE EPCHLHYDKD MTVVCMEGPQ FSTRAESKMY RMFGGHVINM SVIPEAKLAR
ECELPYQMIC MSTDYDAWRD EAEPVTVETV IGNLTNNGRN ANILASKIIV SMAKEIPEFM
HTGDGLRGSI KKSISTKPEA MSKETLERLR YLFPNYW
