MTIP_PSEAE
ID MTIP_PSEAE Reviewed; 245 AA.
AC Q9HZK1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=S-methyl-5'-thioinosine phosphorylase;
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=PA3004;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=21197954; DOI=10.1021/bi101642d;
RA Guan R., Ho M.-C., Almo S.C., Schramm V.L.;
RT "Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and
RT annotation of a novel enzyme in quorum sensing.";
RL Biochemistry 50:1247-1254(2011).
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. Involved in
CC quorum sensing. {ECO:0000255|HAMAP-Rule:MF_01963,
CC ECO:0000269|PubMed:21197954}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for S-methyl-5'-thioinosine {ECO:0000269|PubMed:21197954};
CC KM=23 uM for inosine {ECO:0000269|PubMed:21197954};
CC KM=90 uM for adenosine {ECO:0000269|PubMed:21197954};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01963,
CC ECO:0000269|PubMed:21197954}.
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}.
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; AE004091; AAG06392.1; -; Genomic_DNA.
DR PIR; F83270; F83270.
DR RefSeq; NP_251694.1; NC_002516.2.
DR RefSeq; WP_003091193.1; NZ_QZGE01000009.1.
DR PDB; 3OZB; X-ray; 2.80 A; A/B/C/D/E/F=1-245.
DR PDBsum; 3OZB; -.
DR AlphaFoldDB; Q9HZK1; -.
DR SMR; Q9HZK1; -.
DR STRING; 287.DR97_4933; -.
DR BindingDB; Q9HZK1; -.
DR ChEMBL; CHEMBL3988593; -.
DR PaxDb; Q9HZK1; -.
DR PRIDE; Q9HZK1; -.
DR EnsemblBacteria; AAG06392; AAG06392; PA3004.
DR GeneID; 880215; -.
DR KEGG; pae:PA3004; -.
DR PATRIC; fig|208964.12.peg.3152; -.
DR PseudoCAP; PA3004; -.
DR HOGENOM; CLU_054456_0_2_6; -.
DR InParanoid; Q9HZK1; -.
DR OMA; ADPFCPE; -.
DR PhylomeDB; Q9HZK1; -.
DR BioCyc; MetaCyc:MON-16355; -.
DR BioCyc; PAER208964:G1FZ6-3056-MON; -.
DR BRENDA; 2.4.2.44; 5087.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000002438; 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 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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..245
FT /note="S-methyl-5'-thioinosine phosphorylase"
FT /id="PRO_0000184551"
FT BINDING 10
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 52..53
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 186
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 209..211
FT /ligand="substrate"
FT SITE 167
FT /note="Important for substrate specificity"
FT SITE 221
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3OZB"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3OZB"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3OZB"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3OZB"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:3OZB"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:3OZB"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3OZB"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3OZB"
FT HELIX 221..243
FT /evidence="ECO:0007829|PDB:3OZB"
SQ SEQUENCE 245 AA; 26266 MW; 3C8442062D0666E6 CRC64;
MSVYAIIGGT GLTQLEGLTL SESLPIETPY GAPSAPLQRG RYAGREVLFL ARHGHPHRFP
PHQVNYRANL WALKQAGAEA VIAVNAVGGI HAAMGTGHLC VPHQLIDYTS GREHTYFAGD
IEHVTHIDFS HPYDEPLRQR LIEALRALGL AHSSHGVYAC TQGPRLETVA EIARLERDGN
DIVGMTGMPE AALARELDLP YACLALVVNP AAGKSAGIIT MAEIEQALHD GIGKVREVLA
RVLAG
