ID F2L250_THEU7 Unreviewed; 282 AA.
AC F2L250;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_01963};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=MTAP {ECO:0000256|HAMAP-Rule:MF_01963};
GN Name=mtnP {ECO:0000256|HAMAP-Rule:MF_01963};
GN OrderedLocusNames=TUZN_1506 {ECO:0000313|EMBL:AEA12977.1};
OS Thermoproteus uzoniensis (strain 768-20).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA12977.1, ECO:0000313|Proteomes:UP000008138};
RN [1] {ECO:0000313|EMBL:AEA12977.1, ECO:0000313|Proteomes:UP000008138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-20 {ECO:0000313|EMBL:AEA12977.1,
RC ECO:0000313|Proteomes:UP000008138};
RX PubMed=21478349; DOI=10.1128/JB.00409-11;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL J. Bacteriol. 193:3156-3157(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=768-20;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL Submitted (MAR-2011) 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:0000256|HAMAP-Rule:MF_01963}.
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:0000256|HAMAP-
CC Rule:MF_01963};
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:0000256|HAMAP-
CC Rule:MF_01963}.
CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP-
CC Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}.
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; CP002590; AEA12977.1; -; Genomic_DNA.
DR RefSeq; WP_013680312.1; NC_015315.1.
DR AlphaFoldDB; F2L250; -.
DR STRING; 999630.TUZN_1506; -.
DR GeneID; 10361030; -.
DR KEGG; tuz:TUZN_1506; -.
DR eggNOG; arCOG01327; Archaea.
DR HOGENOM; CLU_054456_0_2_2; -.
DR OrthoDB; 7681at2157; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000008138; Chromosome.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
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:SF3; 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 Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT DOMAIN 24..261
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 30
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 72..73
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 105..106
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 205
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 228..230
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 185
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 240
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 282 AA; 31122 MW; FAAB10FC6402CF83 CRC64;
MKVVKVTSTP VAAKDLGIDE LPAVAIIGGS GLYDPGIFES PVEVQMHTPY GLPSDNVIVG
RVGGRWVAFL PRHGRGHKYP PHRIPYRANI YALHALGVRH VIAVSAVGSL RQDYAPGDFV
VPDQFVDMTK SREYTFYDGP RTCHVQIGLE PFTEELRKAL IEAASKYNKV HTSGCYVCIE
GPRFSTKAES RIWRDVYGCD IIGMTLVPEI NLARELGMCY ALLALVTDYD IWVPHQPVTA
EAVEKMMSEK MDIVRRVVAE VVPKIPSGVE AKCKAVLENA CV
//
