MTAP_BOVIN
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 03-AUG-2022, entry version 97.
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; Q3MHF7; -.
DR PRIDE; Q3MHF7; -.
DR Ensembl; ENSBTAT00000048509; ENSBTAP00000045533; ENSBTAG00000025929.
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; 1616485at2759; -.
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 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; -; 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 PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 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
