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 29-MAY-2024, entry version 93. 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, ECO:0000269|PubMed:31950558}; 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, ECO:0000303|PubMed:31950558}; GN OrderedLocusNames=Rru_A0361; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / OS NCIMB 8255 / S1). OC Bacteria; Pseudomonadota; 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 / NCIMB 8255 / S1; RX PubMed=21886856; DOI=10.4056/sigs.1804360; RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K., RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C., RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y., RA Roberts G.P., Reslewic S., Schwartz D.C.; RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1)."; RL Stand. Genomic Sci. 4:293-302(2011). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION RP PHENOTYPE. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 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). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION RP PHENOTYPE. RX PubMed=31950558; DOI=10.1111/mmi.14459; RA North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A., RA Tabita F.R.; RT "A bifunctional salvage pathway for two distinct S-adenosylmethionine by- RT products that is widespread in bacteria, including pathogenic Escherichia RT coli."; RL Mol. Microbiol. 113:923-937(2020). CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- CC thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate CC (PubMed:23042035, PubMed:31950558). Involved in the breakdown of MTA, a CC major by-product of polyamine biosynthesis. Responsible for the first CC step in the methionine salvage pathway after MTA has been generated CC from S-adenosylmethionine. Has broad substrate specificity with 6- CC aminopurine nucleosides as preferred substrates (By similarity). Also CC catalyzes the phosphorylation of 5'-deoxyadenosine (5'dAdo) to 5- CC deoxyribose 1-phosphate (PubMed:31950558). Part of a bifunctional DHAP- CC shunt salvage pathway for SAM by-products (PubMed:31950558). CC {ECO:0000255|HAMAP-Rule:MF_01963, ECO:0000269|PubMed:23042035, CC ECO:0000269|PubMed:31950558}. 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, ECO:0000269|PubMed:23042035, CC ECO:0000269|PubMed:31950558}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; CC Evidence={ECO:0000269|PubMed:31950558}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5'-deoxyadenosine + phosphate = 5-deoxy-alpha-D-ribose 1- CC phosphate + adenine; Xref=Rhea:RHEA:24869, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:43474, ChEBI:CHEBI:58749; EC=2.4.2.28; CC Evidence={ECO:0000269|PubMed:31950558}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24870; CC Evidence={ECO:0000269|PubMed:31950558}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14 uM for 5'-methylthioadenosine {ECO:0000269|PubMed:23042035}; CC KM=40 uM for 5'-deoxyadenosine {ECO:0000269|PubMed:23042035}; CC KM=41 uM for adenine {ECO:0000269|PubMed:31950558}; CC Note=kcat is 4.5 sec(-1) with 5'-methylthioadenosine as substrate. CC kcat is 6.7 sec(-1) with 5'-deoxyadenosine as substrate CC (PubMed:23042035). kcat is 0.06 sec(-1) with adenine as substrate CC (PubMed:31950558). {ECO:0000269|PubMed:23042035, CC ECO:0000269|PubMed:31950558}; 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 -!- DISRUPTION PHENOTYPE: Mutant cannot release methanethiol upon 5'- CC methylthioadenosine (MTA) feeding (PubMed:23042035). Deletion mutant CC accumulates both MTA and 5'-deoxyadenosine extracellularly CC (PubMed:31950558). {ECO:0000269|PubMed:23042035, CC ECO:0000269|PubMed:31950558}. 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 AlphaFoldDB; Q2RXH9; -. DR SMR; Q2RXH9; -. DR STRING; 269796.Rru_A0361; -. DR EnsemblBacteria; ABC21166; ABC21166; Rru_A0361. DR KEGG; rru:Rru_A0361; -. DR PATRIC; fig|269796.9.peg.417; -. DR eggNOG; COG0005; Bacteria. DR HOGENOM; CLU_054456_0_1_5; -. DR PhylomeDB; Q2RXH9; -. DR BioCyc; MetaCyc:MONOMER-17874; -. DR UniPathway; UPA00904; UER00873. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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: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 1: Evidence at protein level; KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase. FT CHAIN 1..294 FT /note="S-methyl-5'-thioadenosine phosphorylase" FT /id="PRO_0000415099" FT BINDING 16 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 58..59 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 91..92 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 190 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 213..215 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT SITE 171 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT SITE 226 FT /note="Important for substrate specificity" FT /evidence="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 //