ID D5VTF9_METIM Unreviewed; 247 AA.
AC D5VTF9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Probable S-methyl-5'-thioinosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE EC=2.4.2.44 {ECO:0000256|HAMAP-Rule:MF_01963};
DE AltName: Full=5'-methylthioinosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=MTI phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=MTIP {ECO:0000256|HAMAP-Rule:MF_01963};
GN OrderedLocusNames=Metin_1209 {ECO:0000313|EMBL:ADG13862.1};
OS Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13862.1, ECO:0000313|Proteomes:UP000002061};
RN [1] {ECO:0000313|EMBL:ADG13862.1, ECO:0000313|Proteomes:UP000002061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanocaldococcus infernus ME.";
RL Submitted (APR-2010) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01963};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|HAMAP-Rule:MF_01963}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01963}.
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DR EMBL; CP002009; ADG13862.1; -; Genomic_DNA.
DR RefSeq; WP_013100607.1; NC_014122.1.
DR AlphaFoldDB; D5VTF9; -.
DR STRING; 573063.Metin_1209; -.
DR GeneID; 9132228; -.
DR KEGG; mif:Metin_1209; -.
DR eggNOG; arCOG01327; Archaea.
DR HOGENOM; CLU_054456_0_2_2; -.
DR OrthoDB; 7681at2157; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000002061; Chromosome.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro.
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; 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 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 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 34..228
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 8
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 42..43
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 171
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 153
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 206
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 247 AA; 28382 MW; 9A42F8B841F96617 CRC64;
MIAIIGGTGM AEILNEGRER IIYTKYGKAK ILEDDNVIIL LRHGLKHNIP PHRINYKANI
YALKLLGVDK ILAINSVGSL KKEIRPGTFF IPNDFMEFTK RRDDTFYNDR VVHVDLTEPY
CPAMRKELKK ILDKFNFEYQ EGVYICTEGP RFETKSEIKF YSNLGDVVGM TGYPEVVLAR
ELGLCYSSLC NVTNYACGIS EDLLSVEEVF ETIKKMEEKI VKVVREFINS NFESCKCREA
YERGIIC
//
