DEOD_BACCE
ID DEOD_BACCE Reviewed; 235 AA.
AC Q5EEL8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 76.
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};
GN Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627};
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10702 / DSM 487 / NBRC 3466 / NCIMB 8122 / NCTC 8035 / FDA 5;
RA Frassetto L., Rinaldo-Matthis A., Allegrini S., Carta M.C., Tozzi M.G.,
RA Sgarrella F.;
RT "Cloning and expression of adenosine phosphorylase of Bacillus cereus NCIB
RT 8122.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION TO 16.
RA Frassetto L., Allegrini S., Sgarrella F.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AY900166; AAW82755.2; -; Genomic_DNA.
DR RefSeq; WP_000110707.1; NZ_WBPP01000015.1.
DR PDB; 3UAV; X-ray; 1.40 A; A=1-235.
DR PDB; 3UAW; X-ray; 1.20 A; A=1-235.
DR PDB; 3UAX; X-ray; 1.20 A; A=1-235.
DR PDB; 3UAY; X-ray; 1.40 A; A=1-235.
DR PDB; 3UAZ; X-ray; 1.40 A; A=1-235.
DR PDBsum; 3UAV; -.
DR PDBsum; 3UAW; -.
DR PDBsum; 3UAX; -.
DR PDBsum; 3UAY; -.
DR PDBsum; 3UAZ; -.
DR AlphaFoldDB; Q5EEL8; -.
DR SMR; Q5EEL8; -.
DR STRING; 1396.DJ87_3215; -.
DR GeneID; 59158254; -.
DR GeneID; 64203093; -.
DR GeneID; 66263486; -.
DR eggNOG; COG0813; Bacteria.
DR OMA; PQCLLCG; -.
DR OrthoDB; 1028277at2; -.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
DR GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd09006; PNP_EcPNPI-like; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1.
DR InterPro; IPR004402; DeoD-type.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR PANTHER; PTHR43691:SF2; PTHR43691:SF2; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR00107; deoD; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Transferase.
FT CHAIN 1..235
FT /note="Purine nucleoside phosphorylase DeoD-type"
FT /id="PRO_0000063115"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT BINDING 4
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P50389"
FT BINDING 20
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:0000250|UniProtKB:P50389"
FT BINDING 24
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:0000250|UniProtKB:P50389"
FT BINDING 43
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P50389"
FT BINDING 87..90
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:0000250|UniProtKB:P50389"
FT BINDING 162
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:0000250|UniProtKB:P50389"
FT BINDING 179..181
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:0000250|UniProtKB:P50389"
FT BINDING 203..204
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:0000250|UniProtKB:P50389"
FT SITE 217
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3UAX"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:3UAW"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:3UAW"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3UAW"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:3UAW"
SQ SEQUENCE 235 AA; 25675 MW; 41A138A380CA3C31 CRC64;
MSVHIEAKQG EIAESILLPG DPLRAKYIAE TFLEDVTCYN NVRGMLGFTG TYKGKRVSVQ
GTGMGVPSIS IYVNELIQSY GVKNLIRVGT CGAIQKDVKV RDVIIAMTAC TDSNMNRLTF
PGFDFAPAAN FDLLKKAYDA GTEKGLHVRV GNVLTADVFY RESMDMVKKL GDYGVLAVEM
ETTALYTLAA KYGVNALSVL TVSDHIFTGE ETTSEERQTT FNEMIEIALD AAIQQ
