DEOD_MYCPI
ID DEOD_MYCPI Reviewed; 42 AA.
AC P47724;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000255|HAMAP-Rule:MF_01627};
DE Short=PNP {ECO:0000255|HAMAP-Rule:MF_01627};
DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627};
DE Flags: Fragment;
GN Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627};
OS Mycoplasma pirum (Mycoplasmoides pirum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=2122;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BER;
RX PubMed=8349569; DOI=10.1128/jb.175.16.5281-5285.1993;
RA Tham T.N., Ferris S., Kovacic R., Montagnier L., Blanchard A.;
RT "Identification of Mycoplasma pirum genes involved in the salvage pathways
RT for nucleosides.";
RL J. Bacteriol. 175:5281-5285(1993).
CC -!- FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N-
CC glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the
CC formation of the corresponding free purine bases and pentose-1-
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_01627}.
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:0000255|HAMAP-Rule:MF_01627};
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:0000255|HAMAP-Rule:MF_01627};
CC -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000255|HAMAP-
CC Rule:MF_01627}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC {ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000305}.
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DR EMBL; L13289; AAA25430.1; -; Genomic_DNA.
DR PIR; A53312; A53312.
DR AlphaFoldDB; P47724; -.
DR SMR; P47724; -.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR SUPFAM; SSF53167; SSF53167; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN <1..42
FT /note="Purine nucleoside phosphorylase DeoD-type"
FT /id="PRO_0000063147"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT BINDING 8..9
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P50389"
FT SITE 22
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT NON_TER 1
SQ SEQUENCE 42 AA; 4658 MW; 406D7A0EDD73372F CRC64;
ALTLLTVSDS LITKESLSSL ERQTTFNTMV KLALEMACEL QK