ID A0A510E6L4_9CREN Unreviewed; 270 AA. AC A0A510E6L4; A0A510DYV1; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 28-JUN-2023, entry version 18. DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963}; DE EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_01963}; DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963}; DE Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963}; DE Short=MTAP {ECO:0000256|HAMAP-Rule:MF_01963}; GN Name=mtnP {ECO:0000256|HAMAP-Rule:MF_01963}; GN ORFNames=IC006_2727 {ECO:0000313|EMBL:BBG25391.1}, IC007_2741 GN {ECO:0000313|EMBL:BBG28185.1}; OS Sulfuracidifex tepidarius. OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfuracidifex. OX NCBI_TaxID=1294262 {ECO:0000313|EMBL:BBG28185.1, ECO:0000313|Proteomes:UP000325030}; RN [1] {ECO:0000313|Proteomes:UP000322983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC-006 {ECO:0000313|Proteomes:UP000322983}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16833."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000325030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC-007 {ECO:0000313|Proteomes:UP000325030}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16834."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BBG28185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IC-006 {ECO:0000313|EMBL:BBG25391.1}, and IC-007 RC {ECO:0000313|EMBL:BBG28185.1}; RA Itoh T., Miura T., Sakai H.D., Kato S., Ohkuma M., Takashina T.; RT "Sulfuracidifex tepidarius gen. nov., sp. nov. and transfer of Sulfolobus RT metallicus Huber and Stetter 1992 to the genus Sulfuracidifex as RT Sulfuracidifex metallicus comb. nov."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2020). 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:0000256|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:0000256|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:0000256|HAMAP- CC Rule:MF_01963}. CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP- CC Rule:MF_01963}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP CC subfamily. {ECO:0000256|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; AP018929; BBG25391.1; -; Genomic_DNA. DR EMBL; AP018930; BBG28185.1; -; Genomic_DNA. DR RefSeq; WP_054845236.1; NZ_AP018930.1. DR RefSeq; WP_054845236.1; NZ_BBCL01000002.1. DR STRING; 1294262.GCA_001316085_00666; -. DR GeneID; 41719011; -. DR KEGG; step:IC006_2727; -. DR OrthoDB; 7681at2157; -. DR UniPathway; UPA00904; UER00873. DR Proteomes; UP000322983; Chromosome. DR Proteomes; UP000325030; 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 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 TIGRFAMs; TIGR01694; MTAP; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_01963}; Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01963}. FT DOMAIN 10..248 FT /note="Nucleoside phosphorylase" FT /evidence="ECO:0000259|Pfam:PF01048" FT BINDING 16 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 58..59 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 91..92 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 191 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT BINDING 214..216 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT SITE 171 FT /note="Important for substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" FT SITE 225 FT /note="Important for substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963" SQ SEQUENCE 270 AA; 30094 MW; A2B2A18DFCEB7C9D CRC64; MLEQKERASV AIIGGSGIYD LSYISDVKEI KVYTPYGSPS DLISVGRMGN VKVAFLPRHG KNHRIPPHMI NYRANIWALK ELGVKWVISV SAVGSLRMDY KPGDFVVPDQ FIDMTKKREY TFFDGPVVAH VSMADPFCNS LRKRLIEKGN SLGIVVHGQG TYICIEGPRF STRAESRVWK DSFKADIIGM TAVPEVNLAC EAQMCYATLA MVTDYDVFAD IPVTAEEVTQ VMKRNTENAK KLVMEVIKDL PESPNREDCS CCSSLENALL //