ID A0A510E6L4_9CREN Unreviewed; 270 AA. AC A0A510E6L4; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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=IC007_2741 {ECO:0000313|EMBL:BBG28185.1}; OS Sulfolobus sp. JCM 16834. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus; unclassified Sulfolobus. OX NCBI_TaxID=2173830 {ECO:0000313|EMBL:BBG28185.1}; RN [1] {ECO:0000313|EMBL:BBG28185.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IC-007 {ECO:0000313|EMBL:BBG28185.1}; 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. 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 CC salvage pathway after MTA has been generated from S- CC adenosylmethionine. Has broad substrate specificity with 6- CC aminopurine nucleosides as preferred substrates. CC {ECO:0000256|HAMAP-Rule:MF_01963}. CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S- CC methyl-5-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 CC salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from CC S-methyl-5'-thioadenosine (phosphorylase route): step 1/1. CC {ECO:0000256|HAMAP-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; AP018930; BBG28185.1; -; Genomic_DNA. DR UniPathway; UPA00904; UER00873. 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 TIGRFAMs; TIGR01694; MTAP; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963}; KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}. FT DOMAIN 10 248 PNP_UDP_1. {ECO:0000259|Pfam:PF01048}. FT REGION 58 59 Phosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_01963}. FT REGION 91 92 Phosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_01963}. FT REGION 214 216 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01963}. FT BINDING 16 16 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_01963}. FT BINDING 190 190 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01963}. FT BINDING 191 191 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_01963}. FT SITE 171 171 Important for substrate specificity. FT {ECO:0000256|HAMAP-Rule:MF_01963}. FT SITE 225 225 Important for substrate specificity. FT {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 //