PURNU_RICPR
ID PURNU_RICPR Reviewed; 240 AA.
AC Q9ZD53;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Purine nucleoside phosphorylase RP494;
DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=Adenosine deaminase RP494;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE AltName: Full=S-methyl-5'-thioadenosine phosphorylase RP494;
DE EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN OrderedLocusNames=RP494;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of
CC adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and
CC the respective free bases, adenine and hypoxanthine. Also catalyzes the
CC phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-
CC 5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase
CC activity. {ECO:0000250|UniProtKB:P84138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate;
CC Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643;
CC Evidence={ECO:0000250|UniProtKB:P84138};
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:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P33644};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P84138};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q1EIR0}.
CC -!- SIMILARITY: Belongs to the purine nucleoside phosphorylase YfiH/LACC1
CC family. {ECO:0000305}.
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DR EMBL; AJ235272; CAA14946.1; -; Genomic_DNA.
DR PIR; H71652; H71652.
DR RefSeq; NP_220870.1; NC_000963.1.
DR RefSeq; WP_004597737.1; NC_000963.1.
DR AlphaFoldDB; Q9ZD53; -.
DR SMR; Q9ZD53; -.
DR STRING; 272947.RP494; -.
DR PRIDE; Q9ZD53; -.
DR EnsemblBacteria; CAA14946; CAA14946; CAA14946.
DR GeneID; 57569618; -.
DR KEGG; rpr:RP494; -.
DR PATRIC; fig|272947.5.peg.503; -.
DR eggNOG; COG1496; Bacteria.
DR HOGENOM; CLU_065784_2_0_5; -.
DR OMA; CFADCVP; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-EC.
DR CDD; cd16833; YfiH; 1.
DR Gene3D; 3.60.140.10; -; 1.
DR InterPro; IPR003730; Cu_polyphenol_OxRdtase.
DR InterPro; IPR038371; Cu_polyphenol_OxRdtase_sf.
DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR PANTHER; PTHR30616; PTHR30616; 1.
DR Pfam; PF02578; Cu-oxidase_4; 1.
DR SUPFAM; SSF64438; SSF64438; 1.
DR TIGRFAMs; TIGR00726; TIGR00726; 1.
PE 3: Inferred from homology;
KW Copper; Hydrolase; Metal-binding; Oxidoreductase; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..240
FT /note="Purine nucleoside phosphorylase RP494"
FT /id="PRO_0000163170"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P84138"
SQ SEQUENCE 240 AA; 27182 MW; E9594F79AF52C464 CRC64;
MEVLIHKSVY YKIFDKTFNN SSHRYIQENH SINEAEILAN IESITNYFKA QDILILNQVH
SNQIVNADEH IVTIPEADGS ITTKKNLVLT VQSADCVPVL LASDDGKIIG VAHAGWQGSI
NNIISNIVTK MIEKGAKNLI AVIGPAIAQS SYEVDDKYYK TFLSKDINNK RFFINSIKEN
HYMFDLPAFV ELKLNESGVK DIKNITEDTY TNPSKYPSKR RSYHMQVPYN EKILSAIVIK
