ID MTAP_RHORT Reviewed; 294 AA. AC Q2RXH9; DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 07-NOV-2018, entry version 72. 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, ECO:0000269|PubMed:23042035}; DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963, ECO:0000303|PubMed:23042035}; DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_01963}; GN Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963}; GN OrderedLocusNames=Rru_A0361; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION RP PHENOTYPE. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1; RX PubMed=23042035; DOI=10.1038/nchembio.1087; RA Erb T.J., Evans B.S., Cho K., Warlick B.P., Sriram J., Wood B.M., RA Imker H.J., Sweedler J.V., Tabita F.R., Gerlt J.A.; RT "A RubisCO-like protein links SAM metabolism with isoprenoid RT biosynthesis."; RL Nat. Chem. Biol. 8:926-932(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 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:0000255|HAMAP-Rule:MF_01963}. CC -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + phosphate = CC adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01963, ECO:0000269|PubMed:23042035}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14 uM for 5'-methylthioadenosine CC {ECO:0000269|PubMed:23042035}; CC KM=40 uM for 5'-deoxyadenosine {ECO:0000269|PubMed:23042035}; CC Note=kcat is 4.5 sec(-1) with 5'-methylthioadenosine as CC substrate. kcat is 6.7 sec(-1) with 5'-deoxyadenosine as CC substrate. {ECO:0000269|PubMed:23042035}; 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:0000255|HAMAP-Rule:MF_01963}. CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000255|HAMAP- CC Rule:MF_01963}. CC -!- DISRUPTION PHENOTYPE: Mutant cannot release methanethiol upon 5'- CC methylthioadenosine (MTA) feeding. {ECO:0000269|PubMed:23042035}. 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; CP000230; ABC21166.1; -; Genomic_DNA. DR RefSeq; WP_011388114.1; NC_007643.1. DR RefSeq; YP_425453.1; NC_007643.1. DR ProteinModelPortal; Q2RXH9; -. DR SMR; Q2RXH9; -. DR STRING; 269796.Rru_A0361; -. DR EnsemblBacteria; ABC21166; ABC21166; Rru_A0361. DR GeneID; 3834648; -. DR KEGG; rru:Rru_A0361; -. DR PATRIC; fig|269796.9.peg.417; -. DR eggNOG; ENOG4107RHB; Bacteria. DR eggNOG; COG0005; LUCA. DR HOGENOM; HOG000228986; -. DR KO; K00772; -. DR OMA; DYDVWAE; -. DR OrthoDB; POG091H0228; -. DR BioCyc; MetaCyc:MONOMER-17874; -. DR UniPathway; UPA00904; UER00873. DR Proteomes; UP000001929; 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 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 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 294 S-methyl-5'-thioadenosine phosphorylase. FT /FTId=PRO_0000415099. FT REGION 58 59 Phosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT REGION 91 92 Phosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT REGION 213 215 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT BINDING 16 16 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT BINDING 189 189 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01963}. FT BINDING 190 190 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT SITE 171 171 Important for substrate specificity. FT {ECO:0000255|HAMAP-Rule:MF_01963}. FT SITE 226 226 Important for substrate specificity. FT {ECO:0000255|HAMAP-Rule:MF_01963}. SQ SEQUENCE 294 AA; 32078 MW; 58481196C7CCFB4B CRC64; MSEAYRQPVL GVIGGSGVYD IDGLEGARWQ TVESPFGDVS DQILRGTLDG LEMAFLPRHG RGHVLAPSDV NYRANIDALK RAGVTEILSV SAVGSLAEDL PPGTFVIADQ FIDRTFAREK SFFGKGLVAH VSMAHPVSAW LGDRVEEVLA DLAIPHRRGG TYLCMEGPQF STLAESNLYR QWGCHVIGMT NMPEAKLARE AEIAYCTVAM VTDFDCWHPD HDHVSVEAVV RVLLQNADKA RSLVKAMPAK LKDRPYPLPD GSHRSLDNAI ITHPDRRNPG MARKLSAVAG RVLG //