ID MTAP_SCHPO Reviewed; 307 AA. AC Q09816; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 132. 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}; GN ORFNames=SPAC16C9.02c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the fission RT yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). 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. {ECO:0000255|HAMAP-Rule:MF_03155}. 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 {ECO:0000255|HAMAP-Rule:MF_03155, CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03155, CC ECO:0000269|PubMed:16823372}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03155}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU329670; CAA91190.1; -; Genomic_DNA. DR PIR; S62472; S62472. DR RefSeq; NP_593076.1; NM_001018473.2. DR AlphaFoldDB; Q09816; -. DR SMR; Q09816; -. DR BioGRID; 278782; 6. DR STRING; 284812.Q09816; -. DR iPTMnet; Q09816; -. DR PaxDb; 4896-SPAC16C9-02c-1; -. DR EnsemblFungi; SPAC16C9.02c.1; SPAC16C9.02c.1:pep; SPAC16C9.02c. DR GeneID; 2542316; -. DR KEGG; spo:SPAC16C9.02c; -. DR PomBase; SPAC16C9.02c; -. DR VEuPathDB; FungiDB:SPAC16C9.02c; -. DR eggNOG; KOG3985; Eukaryota. DR HOGENOM; CLU_054456_0_1_1; -. DR InParanoid; Q09816; -. DR OMA; ADPFCPE; -. DR PhylomeDB; Q09816; -. DR Reactome; R-SPO-1237112; Methionine salvage pathway. DR UniPathway; UPA00904; UER00873. DR PRO; PR:Q09816; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA:PomBase. DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central. 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; Nucleoside phosphorylase domain; 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 NCBIfam; TIGR01694; MTAP; 1. DR PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1. DR PANTHER; PTHR42679:SF2; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1..307 FT /note="S-methyl-5'-thioadenosine phosphorylase" FT /id="PRO_0000184557" FT BINDING 16 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT BINDING 59..60 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT BINDING 92..93 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT BINDING 199 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT BINDING 222..224 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT SITE 180 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" FT SITE 235 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155" SQ SEQUENCE 307 AA; 33848 MW; A289285BFD438067 CRC64; MNKQAEPILL GVIGGSGFYD LPGFDIVESV NPITPWGYPA SPISIARTTS GFLIAFLARH GVGHIYTPTE VPSRANIAAL KSLGVLAIVS FSAVGSLRED IPPEDFVLPT QIIDRTLCAR PNTFFESGCV AHVSFGDPFD QDLYEILSSC GSNLKNGSKL HTKRKGDDLT VVCMEGPAFS TRAESNLYRS WGASIINMSV IPEAKLAREA EIAYQMVCMA TDYDCWRMNE EPVTVETVME HISNNKDNAK IFLLEAVKKL EAPLLQGFLG RNLRESVQNG IQTNHKHRNP DAIRRLQFLF PNLTIPH //