ID MTAP_LEPIN Reviewed; 287 AA. AC Q8CXR2; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 102. 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}; DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_01963}; GN Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963}; GN OrderedLocusNames=LA_4248; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain OS 56601). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=189518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira interrogans RT revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). 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}; 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 -!- 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; AE010300; AAN51446.1; -; Genomic_DNA. DR RefSeq; NP_714428.1; NC_004342.2. DR RefSeq; WP_000121285.1; NC_004342.2. DR AlphaFoldDB; Q8CXR2; -. DR SMR; Q8CXR2; -. DR STRING; 189518.LA_4248; -. DR PaxDb; 189518-LA_4248; -. DR EnsemblBacteria; AAN51446; AAN51446; LA_4248. DR KEGG; lil:LA_4248; -. DR PATRIC; fig|189518.3.peg.4221; -. DR HOGENOM; CLU_054456_0_2_12; -. DR InParanoid; Q8CXR2; -. DR OrthoDB; 1523230at2; -. DR UniPathway; UPA00904; UER00873. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central. 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 3: Inferred from homology; KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase. FT CHAIN 1..287 FT /note="S-methyl-5'-thioadenosine phosphorylase" FT /id="PRO_0000184550" FT BINDING 13 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 55..56 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 187 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT BINDING 210..212 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT SITE 168 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" FT SITE 223 FT /note="Important for substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963" SQ SEQUENCE 287 AA; 32031 MW; 2830C5FB62F3AE88 CRC64; MSYNVRAAII GGTGLYSLEG MELIEEIFPD TPWGKPSDKI KIGKYKGKLI AFLPRHGIGH FLSPPEVPNH ANICALKQLG VEEIVAFSSV GSLREEIKPL DFVLPSQIID RTRFRNSTYF GNGVVAHAPF AEPFSPNLSK RIAQTAKKIG LEIHLDKTLV CMEGPLFSTK AESHLYRSWG ADIINMTVLP EAKLAREAEI AYQMICMSTD YDCWREGEES VTVEMVIANL TKNAETAKKL LSELIHVLGN GDDLSLKNST RYSIITAPEK RNSETVKKLR VLFPEYF //