PNPH_SACS2
ID PNPH_SACS2 Reviewed; 236 AA.
AC P50389;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Purine nucleoside phosphorylase;
DE Short=PNP;
DE EC=2.4.2.1 {ECO:0000269|PubMed:15819883};
DE AltName: Full=5'-methylthioadenosine phosphorylase I {ECO:0000303|PubMed:8774706};
DE Short=MTA phosphorylase I;
DE Short=MTAPI;
DE EC=2.4.2.28 {ECO:0000269|PubMed:15819883, ECO:0000269|PubMed:7929153};
GN OrderedLocusNames=SSO2706;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8774706; DOI=10.1111/j.1432-1033.1996.0632u.x;
RA Cacciapuoti G., Porcelli M., Bertoldo C., Fusco S., De Rosa M., Zappia V.;
RT "Extremely thermophilic and thermostable 5'-methylthioadenosine
RT phosphorylase from the archaeon Sulfolobus solfataricus. Gene cloning and
RT amino acid sequence determination.";
RL Eur. J. Biochem. 239:632-637(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-26, FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=7929153; DOI=10.1016/s0021-9258(17)31457-6;
RA Cacciapuoti G., Porcelli M., Bertoldo C., de Rosa M., Zappia V.;
RT "Purification and characterization of extremely thermophilic and
RT thermostable 5'-methylthioadenosine phosphorylase from the archaeon
RT Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and
RT evidence for intersubunit disulfide bonds.";
RL J. Biol. Chem. 269:24762-24769(1994).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15819883; DOI=10.1111/j.1742-4658.2005.04619.x;
RA Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.;
RT "A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase
RT from the archaeon Sulfolobus solfataricus.";
RL FEBS J. 272:1886-1899(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND
RP SUBSTRATE ANALOGS, AND DISULFIDE BOND.
RX PubMed=11489901; DOI=10.1074/jbc.m105694200;
RA Appleby T.C., Mathews I.I., Porcelli M., Cacciapuoti G., Ealick S.E.;
RT "Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-
RT methylthioadenosine phosphorylase from Sulfolobus solfataricus.";
RL J. Biol. Chem. 276:39232-39242(2001).
CC -!- FUNCTION: Cleavage of guanosine or inosine to respective bases and
CC sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine
CC with a better efficiency than MTA. {ECO:0000269|PubMed:15819883,
CC ECO:0000269|PubMed:7929153}.
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;
CC Evidence={ECO:0000269|PubMed:15819883, ECO:0000269|PubMed:7929153};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:15819883, ECO:0000269|PubMed:7929153};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC alpha-D-ribose 1-phosphate + a purine nucleobase;
CC Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:15819883};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=154 uM for S-methyl-5'-thioadenosine
CC {ECO:0000269|PubMed:15819883};
CC KM=25.4 uM for adenosine {ECO:0000269|PubMed:15819883};
CC KM=84 uM for inosine {ECO:0000269|PubMed:15819883};
CC KM=113.6 uM for guanosine {ECO:0000269|PubMed:15819883};
CC Temperature dependence:
CC Optimum temperature is 120 degrees Celsius. Highly thermostable.
CC {ECO:0000269|PubMed:15819883};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC -!- SUBUNIT: Homohexamer; disulfide-linked. Trimer of homodimers, with
CC three symmetric intersubunit disulfide bonds linking the dimers to one
CC another. {ECO:0000269|PubMed:11489901, ECO:0000269|PubMed:7929153}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
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DR EMBL; Z50181; CAA90560.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42818.1; -; Genomic_DNA.
DR PIR; S58291; S58291.
DR RefSeq; WP_009988635.1; NC_002754.1.
DR PDB; 1JDS; X-ray; 1.80 A; A/B/C/D/E/F=1-236.
DR PDB; 1JDT; X-ray; 2.00 A; A/B/C=1-236.
DR PDB; 1JDU; X-ray; 2.50 A; A/B/C=1-236.
DR PDB; 1JDV; X-ray; 2.00 A; A/B/C/D/E/F=1-236.
DR PDB; 1JDZ; X-ray; 2.00 A; A/B/C=1-236.
DR PDB; 1JE0; X-ray; 1.60 A; A/B/C=1-236.
DR PDB; 1JE1; X-ray; 1.80 A; A/B/C/D/E/F=1-236.
DR PDB; 1JP7; X-ray; 1.80 A; A/B/C=1-236.
DR PDB; 1JPV; X-ray; 1.80 A; A/B/C=1-236.
DR PDBsum; 1JDS; -.
DR PDBsum; 1JDT; -.
DR PDBsum; 1JDU; -.
DR PDBsum; 1JDV; -.
DR PDBsum; 1JDZ; -.
DR PDBsum; 1JE0; -.
DR PDBsum; 1JE1; -.
DR PDBsum; 1JP7; -.
DR PDBsum; 1JPV; -.
DR AlphaFoldDB; P50389; -.
DR SMR; P50389; -.
DR STRING; 273057.SSO2706; -.
DR ChEMBL; CHEMBL3751658; -.
DR EnsemblBacteria; AAK42818; AAK42818; SSO2706.
DR GeneID; 44128433; -.
DR KEGG; sso:SSO2706; -.
DR PATRIC; fig|273057.12.peg.2787; -.
DR eggNOG; arCOG01324; Archaea.
DR HOGENOM; CLU_068457_0_1_2; -.
DR InParanoid; P50389; -.
DR OMA; PQCLLCG; -.
DR PhylomeDB; P50389; -.
DR BRENDA; 2.4.2.28; 6163.
DR UniPathway; UPA00606; -.
DR EvolutionaryTrace; P50389; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004850; F:uridine phosphorylase activity; IBA:GO_Central.
DR GO; GO:0006218; P:uridine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..236
FT /note="Purine nucleoside phosphorylase"
FT /id="PRO_0000063195"
FT BINDING 5
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11489901"
FT BINDING 21
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11489901,
FT ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JE0"
FT BINDING 25
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11489901,
FT ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JE0"
FT BINDING 43
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11489901,
FT ECO:0007744|PDB:1JE0"
FT BINDING 86..89
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11489901,
FT ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JE0"
FT BINDING 163
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11489901"
FT BINDING 180..182
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11489901,
FT ECO:0007744|PDB:1JDT, ECO:0007744|PDB:1JE1"
FT BINDING 204..205
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11489901"
FT DISULFID 125
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:11489901,
FT ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JDT,
FT ECO:0007744|PDB:1JDU, ECO:0007744|PDB:1JDV,
FT ECO:0007744|PDB:1JDZ, ECO:0007744|PDB:1JE0,
FT ECO:0007744|PDB:1JE1, ECO:0007744|PDB:1JP7,
FT ECO:0007744|PDB:1JPV"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1JDV"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1JE1"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:1JE0"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1JE0"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:1JE0"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:1JE0"
SQ SEQUENCE 236 AA; 25738 MW; F1570ECE8AA3D51B CRC64;
MNPVHILAKK GEVAERVLVV GDPGRARLLS TLLQNPKLTN ENRGFLVYTG KYNGETVSIA
THGIGGPSIA IVLEELAMLG ANVFIRYGTT GALVPYINLG EYIIVTGASY NQGGLFYQYL
RDNACVASTP DFELTNKLVT SFSKRNLKYY VGNVFSSDAF YAEDEEFVKK WSSRGNIAVE
MECATLFTLS KVKGWKSATV LVVSDNLAKG GIWITKEELE KSVMDGAKAV LDTLTS
