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PURNU_STAAU
ID   PURNU_STAAU             Reviewed;         263 AA.
AC   Q9ZHA4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Purine nucleoside phosphorylase YlmD;
DE            EC=2.4.2.1 {ECO:0000250|UniProtKB:P84138};
DE   AltName: Full=Adenosine deaminase YlmD;
DE            EC=3.5.4.4 {ECO:0000250|UniProtKB:P84138};
DE   AltName: Full=S-methyl-5'-thioadenosine phosphorylase YlmD;
DE            EC=2.4.2.28 {ECO:0000250|UniProtKB:P84138};
GN   Name=ylmD;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14154 / Rose;
RX   PubMed=9846742; DOI=10.1099/00221287-144-11-3069;
RA   Massidda O., Anderluzzi D., Friedli L., Feger G.;
RT   "Unconventional organization of the division and cell wall gene cluster of
RT   Streptococcus pneumoniae.";
RL   Microbiology 144:3069-3078(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; AF068904; AAC95459.1; -; Genomic_DNA.
DR   RefSeq; WP_000999333.1; NZ_NGNJ01000001.1.
DR   AlphaFoldDB; Q9ZHA4; -.
DR   SMR; Q9ZHA4; -.
DR   OMA; CFADCVP; -.
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; Transferase; Zinc.
FT   CHAIN           1..263
FT                   /note="Purine nucleoside phosphorylase YlmD"
FT                   /id="PRO_0000163177"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P84138"
SQ   SEQUENCE   263 AA;  30097 MW;  76A0DA0EBFCD62AD CRC64;
     MNDNFKKQPH HLIYEELLQQ GITLGITTRG DGLSDYPKNA FNMARYIDDC PYNITQHQLQ
     LAEEIAFDRK NWVFPIQTHE NKVACITKDD IGTNIDTLTD ALHGIDAMYT YDSNVLLTMC
     YADCVPVYFY STKHHFIALA HAGWRGTYTE IVKEVLKHVN FDLKDLHVVI GPSTSSSYEI
     NDDIKNKFET LPIDSANYIE TRGRDRHGID LKKANAALLN NYGVPKENIY TTAYATSEHL
     ELFFSYRLEK GQTGRMLAFI GQQ
 
 
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