ID MTAP_PYRAB Reviewed; 257 AA. AC Q9V2F1; G8ZFV8; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE EC=2.4.2.28 {ECO:0000255|HAMAP-Rule:MF_01963}; DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_01963}; GN Name=mntP; Synonyms=mtaP; OrderedLocusNames=PYRAB01230; GN ORFNames=PAB2264; OS Pyrococcus abyssi (strain GE5 / Orsay). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=272844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay; RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., RA Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic archaeon RT Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). RN [2] RP GENOME REANNOTATION. RC STRAIN=GE5 / Orsay; RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x; RA Gao J., Wang J.; RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and RT Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(2012). 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_01963}. 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_01963}; 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_01963}. CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000255|HAMAP- CC Rule:MF_01963}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}. 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; AJ248283; CAB49047.1; -; Genomic_DNA. DR EMBL; HE613800; CCE69499.1; -; Genomic_DNA. DR PIR; H75199; H75199. DR RefSeq; WP_010867247.1; NC_000868.1. DR AlphaFoldDB; Q9V2F1; -. DR SMR; Q9V2F1; -. DR STRING; 272844.PAB2264; -. DR GeneID; 1495010; -. DR KEGG; pab:PAB2264; -. DR PATRIC; fig|272844.11.peg.136; -. DR eggNOG; arCOG01327; Archaea. DR HOGENOM; CLU_054456_0_2_2; -. DR OrthoDB; 7681at2157; -. DR PhylomeDB; Q9V2F1; -. DR UniPathway; UPA00904; UER00873. DR Proteomes; UP000000810; Chromosome. DR Proteomes; UP000009139; Chromosome. DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule. 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:SF3; 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 Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1..257 FT /note="S-methyl-5'-thioadenosine phosphorylase" FT /id="PRO_0000184560" FT BINDING 10 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 50..51 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 181 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 204..206 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT SITE 163 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT SITE 215 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" SQ SEQUENCE 257 AA; 29172 MW; E0C651C18B63A15C CRC64; MPKIGIIGGS GVYGVFEPKE VVKIHTPYGR PSAPVEIGEI EGVEVAFIPR HGKYHEFPPH EVPYRANIWA LYELGVERII AINAVGSLKE EYKPGDIVII DQFIDFTKKR EYTFYNGPKV AHVSMADPFC PELRRIFIET AKELGLPVHE KGTYICIEGP RFSTRAESRM FRQFADVIGM TLVPEVNLAR ELGMCYVNIS TVTDYDVWAE KPVNAQEVLR VMKENEEKVQ KLLRKAIPKI PEERKCGCAD VLKTMFV //