DEOD_YERPY
ID DEOD_YERPY Reviewed; 239 AA.
AC B1JL34;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; OrderedLocusNames=YPK_3624;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) 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; CP000950; ACA69891.1; -; Genomic_DNA.
DR RefSeq; WP_011191689.1; NZ_CP009792.1.
DR PDB; 3OCC; X-ray; 1.70 A; A/B/C/D/E/F=1-239.
DR PDBsum; 3OCC; -.
DR AlphaFoldDB; B1JL34; -.
DR SMR; B1JL34; -.
DR EnsemblBacteria; ACA69891; ACA69891; YPK_3624.
DR GeneID; 66842995; -.
DR KEGG; ypy:YPK_3624; -.
DR PATRIC; fig|502800.11.peg.4376; -.
DR OMA; PQCLLCG; -.
DR EvolutionaryTrace; B1JL34; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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..239
FT /note="Purine nucleoside phosphorylase DeoD-type"
FT /id="PRO_1000186245"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT BINDING 5
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 21
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 25
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 44
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 88..91
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 180..182
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 204..205
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 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:3OCC"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:3OCC"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:3OCC"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3OCC"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:3OCC"
SQ SEQUENCE 239 AA; 25936 MW; 344A15BFAA7F7975 CRC64;
MATPHINAEM GDFADVVLMP GDPLRAKFIA ETFLQDVREV NNVRGMLGFT GTYKGRKISV
MGHGMGIPSC SIYAKELITD FGVKKIIRVG SCGAVRTDVK LRDVVIGMGA CTDSKVNRMR
FKDHDYAAIA DFEMTRNAVD AAKAKGVNVR VGNLFSADLF YTPDPQMFDV MEKYGILGVE
MEAAGIYGVA AEFGAKALTI CTVSDHIRTG EQTTAAERQT TFNDMIEIAL ESVLLGDNA
