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 26-FEB-2020, entry version 78. 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}; OrderedLocusNames=Rru_A0361; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / OS 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; 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 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 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, ECO:0000269|PubMed:23042035}; 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 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 {ECO:0000269|PubMed:23042035}; 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. {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 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; CLU_054456_0_1_5; -. DR KO; K00772; -. DR OMA; DYDVWAE; -. DR OrthoDB; 1364220at2; -. 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 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 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 REGION 58..59 FT /note="Phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT REGION 91..92 FT /note="Phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT REGION 213..215 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 16 FT /note="Phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 189 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 190 FT /note="Phosphate" 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 //