ID MTAP_LEPIC Reviewed; 287 AA. AC Q72LZ4; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 99. 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=LIC_13399; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni OS (strain Fiocruz L1-130). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=267671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fiocruz L1-130; RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004; RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T., RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.; RT "Comparative genomics of two Leptospira interrogans serovars reveals novel RT insights into physiology and pathogenesis."; RL J. Bacteriol. 186:2164-2172(2004). 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; AE016823; AAS71939.1; -; Genomic_DNA. DR RefSeq; WP_000121286.1; NC_005823.1. DR AlphaFoldDB; Q72LZ4; -. DR SMR; Q72LZ4; -. DR GeneID; 61143264; -. DR KEGG; lic:LIC_13399; -. DR HOGENOM; CLU_054456_0_1_12; -. DR UniPathway; UPA00904; UER00873. DR Proteomes; UP000007037; Chromosome I. 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 3: Inferred from homology; KW Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1..287 FT /note="S-methyl-5'-thioadenosine phosphorylase" FT /id="PRO_0000184549" 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; 32069 MW; 2DE328C06A622457 CRC64; MSYNVRVAII 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 RNPETVKKLR VLFPEYF //