ID   MTAP_BOVIN              Reviewed;         283 AA.
AC   Q3MHF7; F1N1J3;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 103.
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   Name=MTAP {ECO:0000255|HAMAP-Rule:MF_03155};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=2108157; DOI=10.1016/s0021-9258(19)39316-0;
RA   Della Ragione F., Oliva A., Gragnaniello V., Russo G.L., Palumbo R.,
RA   Zappia V.;
RT   "Physicochemical and immunological studies on mammalian 5'-deoxy-5'-
RT   methylthioadenosine phosphorylase.";
RL   J. Biol. Chem. 265:6241-6246(1990).
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       ECO:0000269|PubMed:2108157}.
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; DAAA02022238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC105254; AAI05255.1; -; mRNA.
DR   RefSeq; XP_002689552.1; XM_002689506.5.
DR   RefSeq; XP_015319924.1; XM_015464438.1.
DR   AlphaFoldDB; Q3MHF7; -.
DR   SMR; Q3MHF7; -.
DR   STRING; 9913.ENSBTAP00000045533; -.
DR   PaxDb; 9913-ENSBTAP00000045533; -.
DR   Ensembl; ENSBTAT00000048509.4; ENSBTAP00000045533.4; ENSBTAG00000025929.5.
DR   GeneID; 782907; -.
DR   KEGG; bta:782907; -.
DR   CTD; 4507; -.
DR   VEuPathDB; HostDB:ENSBTAG00000025929; -.
DR   eggNOG; KOG3985; Eukaryota.
DR   GeneTree; ENSGT00950000182991; -.
DR   InParanoid; Q3MHF7; -.
DR   OMA; ADPFCPE; -.
DR   OrthoDB; 168017at2759; -.
DR   Reactome; R-BTA-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000025929; Expressed in conceptus and 106 other cell types or tissues.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..283
FT                   /note="S-methyl-5'-thioadenosine phosphorylase"
FT                   /id="PRO_0000415112"
FT   BINDING         18
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         60..61
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         93..94
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         197
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         220..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            178
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            233
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   MOD_RES         51
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ65"
SQ   SEQUENCE   283 AA;  31256 MW;  9618D53A124CA360 CRC64;
     MSSGATPAAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALVLGKI KNVDCVLLAR
     HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLKE EIQPGDIIII DQFIDRTTRR
     LQTFYDGNHS CARGVCHIPM AEPFCPKTRE VLIETAKKLG LRCHSKGTMI TIEGPRFSSR
     AESIMFQTWG ADVINMTTVP EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL
     KENANKAKSL LLTTIPQIGS MEWSETLHNM KKMAQFSVLL PRH
//