ID A0A1G4VYF8_9FIRM Unreviewed; 242 AA.
AC A0A1G4VYF8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000256|HAMAP-Rule:MF_01627};
DE Short=PNP {ECO:0000256|HAMAP-Rule:MF_01627};
DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01627};
GN Name=deoD {ECO:0000256|HAMAP-Rule:MF_01627};
GN ORFNames=SAMN02910339_01912 {ECO:0000313|EMBL:SCX13786.1};
OS Lachnospiraceae bacterium YSD2013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX13786.1, ECO:0000313|Proteomes:UP000199278};
RN [1] {ECO:0000313|EMBL:SCX13786.1, ECO:0000313|Proteomes:UP000199278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSD2013 {ECO:0000313|EMBL:SCX13786.1,
RC ECO:0000313|Proteomes:UP000199278};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001020};
CC -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000256|HAMAP-
CC Rule:MF_01627}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC {ECO:0000256|HAMAP-Rule:MF_01627}.
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DR EMBL; FMTX01000016; SCX13786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4VYF8; -.
DR STRING; 1520828.SAMN02910339_01912; -.
DR OrthoDB; 9782889at2; -.
DR Proteomes; UP000199278; Unassembled WGS sequence.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:RHEA.
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; Nucleoside phosphorylase domain; 1.
DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1.
DR InterPro; IPR004402; DeoD-type.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR NCBIfam; TIGR00107; deoD; 1.
DR PANTHER; PTHR43691:SF11; FI09636P-RELATED; 1.
DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01627}; Reference proteome {ECO:0000313|Proteomes:UP000199278};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01627}.
FT DOMAIN 19..230
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 8
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
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:0000256|HAMAP-Rule:MF_01627"
FT BINDING 28
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:0000256|HAMAP-Rule:MF_01627"
FT BINDING 47
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
FT BINDING 91..94
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:0000256|HAMAP-Rule:MF_01627"
FT BINDING 183..185
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:0000256|HAMAP-Rule:MF_01627"
FT BINDING 207..208
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:0000256|HAMAP-Rule:MF_01627"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01627"
SQ SEQUENCE 242 AA; 26380 MW; CCDE6825138854D2 CRC64;
MANYPTPHIN AKPEDFAKTV LMPGDPLRSK FIAENFLENP VLVNNVRGVQ GYTGTYKGTK
VTVMASGMGM PSIGIYSYEL FNFFGVENII RIGSAGSLSK DIKIRDIVFG MGACTNSDYA
RQFNLPGTLA CTADYTLLKT AIAEADNLKA RYHVGNVVSS DTFYDADPTV NDRWASMGAM
AVEMEAAALY MNAIKAKKRA LAILTISDNI MTGEATTAEE RQTSFTQMME VALNTAVQMD
KM
//
