MTIP_THEYD
ID MTIP_THEYD Reviewed; 265 AA.
AC B5YKP5;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable S-methyl-5'-thioinosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE EC=2.4.2.44 {ECO:0000255|HAMAP-Rule:MF_01963};
DE AltName: Full=5'-methylthioinosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE Short=MTI phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE Short=MTIP {ECO:0000255|HAMAP-Rule:MF_01963};
GN OrderedLocusNames=THEYE_A0977;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate.
CC Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major
CC by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via
CC deamination to MTI and phosphorolysis to hypoxanthine.
CC {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-
CC 5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:30643,
CC ChEBI:CHEBI:17368, ChEBI:CHEBI:43474, ChEBI:CHEBI:48595,
CC ChEBI:CHEBI:58533; EC=2.4.2.44; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01963};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC phosphorylases based on sequence homology, it has been shown that
CC conserved amino acid substitutions in the substrate binding pocket
CC convert the substrate specificity of this enzyme from 6-aminopurines to
CC 6-oxopurines. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
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DR EMBL; CP001147; ACI21697.1; -; Genomic_DNA.
DR RefSeq; WP_012546405.1; NC_011296.1.
DR RefSeq; YP_002248810.1; NC_011296.1.
DR AlphaFoldDB; B5YKP5; -.
DR SMR; B5YKP5; -.
DR STRING; 289376.THEYE_A0977; -.
DR EnsemblBacteria; ACI21697; ACI21697; THEYE_A0977.
DR KEGG; tye:THEYE_A0977; -.
DR PATRIC; fig|289376.4.peg.962; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_0_2_0; -.
DR InParanoid; B5YKP5; -.
DR OMA; ADPFCPE; -.
DR OrthoDB; 1364220at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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-UniRule.
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 PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..265
FT /note="Probable S-methyl-5'-thioinosine phosphorylase"
FT /id="PRO_0000415139"
FT BINDING 15
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 55..56
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 188
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 169
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 223
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ SEQUENCE 265 AA; 29620 MW; B109DB0BD2497606 CRC64;
MHNKQQVKIG IIGGSGLSES EAKKEIITIK TPYGEPSCPY EIEKIDDIEV LFLRRHGQKH
SIPPHKVNYR ANIYGFKNFG IERIFGVFAT GSLTENIPPG SIVIPNQIID FTQGMRANTF
YEEKKVVHID FTEPFCSEIR HYLLETARKI GINVISHATY ICVNGPRLET AAEIKFFKNI
GADIIGMTIM PEASLAREVE ICYAAVAVVA NYAAGISKFP LTVKEVIETM EDSLDAVGFL
IKETIKKLPE ERKCLCKHAL KNASF
