ID   MTAP_SYNYG              Reviewed;         326 AA.
AC   P0DJF9; P74469;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   13-SEP-2023, entry version 48.
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=SYNGTS_1998;
OS   Synechocystis sp. (strain PCC 6803 / GT-S).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111707;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / GT-S;
RX   PubMed=21803841; DOI=10.1093/dnares/dsr026;
RA   Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K.,
RA   Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.;
RT   "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain
RT   GT-S.";
RL   DNA Res. 18:393-399(2011).
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}.
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DR   EMBL; AP012205; BAK50746.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DJF9; -.
DR   SMR; P0DJF9; -.
DR   KEGG; syy:SYNGTS_1998; -.
DR   PATRIC; fig|1148.106.peg.2221; -.
DR   UniPathway; UPA00904; UER00873.
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   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.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Purine salvage; Transferase.
FT   CHAIN           1..326
FT                   /note="S-methyl-5'-thioadenosine phosphorylase"
FT                   /id="PRO_0000416437"
FT   BINDING         44
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         86..87
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         119..120
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         221
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         244..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            202
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            257
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   326 AA;  35319 MW;  06F7D98E67A7BCD8 CRC64;
     MGMIISMAMT AVTIWTKTKP GRVSCFIRKN STMVNAPIGI IGGSGLYQME ALKNVEEVTL
     DTPFGAPSDS FIVGELAGVR VAFLARHGRG HHLLPSEIPF RANIHGMKQL GVKYLISASA
     VGSLQAEAKP LDMVVPDQFI DRTRQRISTF FGEGIVAHIG FGNPICPQLA QCLSTAIAGL
     ELEGVTLHDR GTYVSMEGPA FSTIAESNLY RSWGGTVIGM TNLPEAKLAR EAEIAYATLA
     LVTDYDCWHP DHDHVTVEMV IGNLQKNAVN AQQVILETVK QLAANPFESI AHRALQYAVL
     TPPDKFPAAT YEKLSLLLGK YYPPAP
//