ID M7PGQ1_9GAMM Unreviewed; 251 AA.
AC M7PGQ1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=MPL1_07134 {ECO:0000313|EMBL:EMR13075.1};
OS Methylophaga lonarensis MPL.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13075.1, ECO:0000313|Proteomes:UP000012019};
RN [1] {ECO:0000313|EMBL:EMR13075.1, ECO:0000313|Proteomes:UP000012019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPL {ECO:0000313|EMBL:EMR13075.1,
RC ECO:0000313|Proteomes:UP000012019};
RX PubMed=23661481;
RA Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA Murrell J.C., Shouche Y.S.;
RT "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT (Non-Methane-Utilizing) Methylotroph.";
RL Genome Announc. 1:E00202-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMR13075.1}.
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; APHR01000035; EMR13075.1; -; Genomic_DNA.
DR RefSeq; WP_009726416.1; NZ_APHR01000035.1.
DR AlphaFoldDB; M7PGQ1; -.
DR STRING; 1286106.MPL1_07134; -.
DR PATRIC; fig|1286106.3.peg.1432; -.
DR eggNOG; COG0005; Bacteria.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000012019; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW Reference proteome {ECO:0000313|Proteomes:UP000012019};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT DOMAIN 5..240
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 11
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 53..54
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 187
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 210..212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 168
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 222
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 251 AA; 27523 MW; FBAE57FD433FCF37 CRC64;
MSQLLAIIGG SGFAELPEFE LISRHEIETP FGSPSAPVMD GLLNGCRILL LPRHGLAHQF
APHKINYRAN LWALHSLGCS RIIAVAAVGG IHLDCAPGKL VLPDQLIDYT WGRESSFFSD
QFSADRHIDF TWPYDEALRN ELMNAAQLCE LEIRPAGTYG ATQGPRLETA AEIARLARDG
CDLVGMTGMP EAVLARELNL PYACCAVVAN YAAGLSDKTL SMSEIERTLA GSMEQVYRLI
NCYTQRLLSR Q
//
