MTAP_CAEEL
ID MTAP_CAEEL Reviewed; 288 AA.
AC Q09438;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=B0228.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; FO080130; CCD61451.1; -; Genomic_DNA.
DR PIR; T29047; T29047.
DR RefSeq; NP_495629.2; NM_063228.6.
DR AlphaFoldDB; Q09438; -.
DR SMR; Q09438; -.
DR BioGRID; 39585; 7.
DR STRING; 6239.B0228.7.1; -.
DR EPD; Q09438; -.
DR PaxDb; Q09438; -.
DR PeptideAtlas; Q09438; -.
DR EnsemblMetazoa; B0228.7.1; B0228.7.1; WBGene00015064.
DR EnsemblMetazoa; B0228.7.2; B0228.7.2; WBGene00015064.
DR UCSC; B0228.7.1; c. elegans.
DR WormBase; B0228.7; CE34630; WBGene00015064; -.
DR eggNOG; KOG3985; Eukaryota.
DR GeneTree; ENSGT00950000182991; -.
DR HOGENOM; CLU_054456_0_0_1; -.
DR InParanoid; Q09438; -.
DR OMA; ADPFCPE; -.
DR OrthoDB; 1616485at2759; -.
DR PhylomeDB; Q09438; -.
DR Reactome; R-CEL-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00873.
DR PRO; PR:Q09438; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00015064; Expressed in larva and 4 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 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000184547"
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 288 AA; 31564 MW; A998E73C52DA1D3C CRC64;
MVKVGIIGGS GLEDPNILLD PVTVAVDTPY GKPSDDVVEG TINGVECVLL ARHGRKHDIM
PGNVNFRANL WALYSRGVDV IIASTACGSL QENVEPGHLL FPDSVFDRTT GRQSTFFDGS
YDQAPGVCHI QAHPTYNEKL RQVLISTAER CQLVHHRTGF GVCIEGPRFS TKAESMVFKS
WGASLVNMTM MPECILAKEL GIPYATTALV TDYDCWKEED HVTASSVMKV FAANVEKAKT
LFVEAVGEIG KIDWSAEILK LKTEARESVM ISPDVVIPFL TTDNQKKF
