ID   MTAP_DANRE              Reviewed;         280 AA.
AC   Q7ZV22; Q6PHI0;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 126.
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; ORFNames=zgc:66012;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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; BX323448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046035; AAH46035.2; -; mRNA.
DR   EMBL; BC056545; AAH56545.1; -; mRNA.
DR   RefSeq; NP_956848.1; NM_200554.1.
DR   AlphaFoldDB; Q7ZV22; -.
DR   SMR; Q7ZV22; -.
DR   STRING; 7955.ENSDARP00000054207; -.
DR   PaxDb; 7955-ENSDARP00000054207; -.
DR   GeneID; 393526; -.
DR   KEGG; dre:393526; -.
DR   AGR; ZFIN:ZDB-GENE-040426-1505; -.
DR   CTD; 4507; -.
DR   ZFIN; ZDB-GENE-040426-1505; mtap.
DR   eggNOG; KOG3985; Eukaryota.
DR   HOGENOM; CLU_054456_0_0_1; -.
DR   InParanoid; Q7ZV22; -.
DR   OMA; ADPFCPE; -.
DR   OrthoDB; 168017at2759; -.
DR   PhylomeDB; Q7ZV22; -.
DR   TreeFam; TF312883; -.
DR   Reactome; R-DRE-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00873.
DR   PRO; PR:Q7ZV22; -.
DR   Proteomes; UP000000437; Chromosome 1.
DR   Bgee; ENSDARG00000037261; Expressed in swim bladder and 27 other cell types or tissues.
DR   ExpressionAtlas; Q7ZV22; baseline and differential.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..280
FT                   /note="S-methyl-5'-thioadenosine phosphorylase"
FT                   /id="PRO_0000415114"
FT   BINDING         15
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         57..58
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         90..91
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         194
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            175
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            230
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
SQ   SEQUENCE   280 AA;  30847 MW;  EBAB6A6FD5663B36 CRC64;
     MTSNSHVKIG IIGGSGLDDP DILEGRTERY VVTPYGKPSD ALILGKIKNV DCVLLARHGR
     QHTIMPTNVN YQANIWALKE EGCTHLLVTT ACGSLREDIQ PGDIVLIDQF IDRTTKRVQT
     FYDGQPTSPP GVCHIPMAEP FCSKTREVLL EVAQGLGVKC HTRGTMVTIE GPRFSSRAES
     LMFRQWGADV INMTTVPEVV LAKEAGLCYA SIAMATDYDC WKEHEEAVCV DNVLKTMKEN
     ANKASSILLT AIPQICQMDW DSTINAHKSM SQSSVMLPKH
//