ID   MTAP_CAEBR              Reviewed;         285 AA.
AC   A8XGS6;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE            EC=2.4.2.28 {ECO:0000255|HAMAP-Rule:MF_03155};
DE   AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE            Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE            Short=MTAP {ECO:0000255|HAMAP-Rule:MF_03155};
DE            Short=MTAPase {ECO:0000255|HAMAP-Rule:MF_03155};
GN   ORFNames=CBG12968;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(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_03155}.
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_03155};
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_03155}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03155}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03155}.
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DR   EMBL; HE600938; CAP31850.1; -; Genomic_DNA.
DR   RefSeq; XP_002630529.1; XM_002630483.1.
DR   AlphaFoldDB; A8XGS6; -.
DR   SMR; A8XGS6; -.
DR   STRING; 6238.A8XGS6; -.
DR   EnsemblMetazoa; CBG12968.1; CBG12968.1; WBGene00033820.
DR   EnsemblMetazoa; CBG12968.2; CBG12968.2; WBGene00033820.
DR   GeneID; 8572045; -.
DR   KEGG; cbr:CBG_12968; -.
DR   CTD; 8572045; -.
DR   WormBase; CBG12968; CBP22764; WBGene00033820; -.
DR   eggNOG; KOG3985; Eukaryota.
DR   HOGENOM; CLU_054456_0_0_1; -.
DR   InParanoid; A8XGS6; -.
DR   OMA; ADPFCPE; -.
DR   OrthoDB; 168017at2759; -.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..285
FT                   /note="S-methyl-5'-thioadenosine phosphorylase"
FT                   /id="PRO_0000415122"
FT   BINDING         10
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         52..53
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         85..86
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         189
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         212..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            170
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            224
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
SQ   SEQUENCE   285 AA;  31011 MW;  2156DCAD3564F43F CRC64;
     MVKVGIIGGS GLEDPNILLN PTAISIDTPY GQPSDHLIQG TINGVECVLL ARHGRKHDIM
     PGNVNYRANL WALYSLGVDV IIASTACGSL KEEVAPGHLL FPDSVFDRTN SRKATFFDGT
     FSGAPGVSHI QAHPTYNEKL RQVLISTAEK CKLVHHRTGF GVCIEGPRFS TKAESMVFKS
     WGASLVNMTM MPECILAKEL GIPYATTALV TDYDCWKDED QVTAASVMKV FAANVEKAKT
     LFIEAVAEIG KIDWSAEILQ TKTAARQSIM ISPDVEVEFL KVPKT
//