ID   DEOD_ECO57              Reviewed;         239 AA.
AC   P0ABP9; P09743;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 110.
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};
GN   OrderedLocusNames=Z5986, ECs5343;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH PURINE NUCLEOSIDES
RP   AND PHOSPHATE.
RX   PubMed=12937174; DOI=10.1074/jbc.m304622200;
RA   Bennett E.M., Li C., Allan P.W., Parker W.B., Ealick S.E.;
RT   "Structural basis for substrate specificity of Escherichia coli purine
RT   nucleoside phosphorylase.";
RL   J. Biol. Chem. 278:47110-47118(2003).
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; AE005174; AAG59565.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38766.1; -; Genomic_DNA.
DR   PIR; A86138; A86138.
DR   PIR; G91296; G91296.
DR   RefSeq; NP_313370.1; NC_002695.1.
DR   RefSeq; WP_000224877.1; NZ_VOAI01000002.1.
DR   PDB; 1PK7; X-ray; 2.50 A; A/B/C=2-238.
DR   PDB; 1PK9; X-ray; 1.90 A; A/B/C=2-238.
DR   PDB; 1PKE; X-ray; 2.30 A; A/B/C=2-238.
DR   PDB; 1PR0; X-ray; 2.20 A; A/B/C=1-239.
DR   PDB; 1PR1; X-ray; 2.30 A; A/B/C=1-239.
DR   PDB; 1PR2; X-ray; 2.30 A; A/B/C=1-239.
DR   PDB; 1PR4; X-ray; 2.40 A; A/B/C=1-239.
DR   PDB; 1PR5; X-ray; 2.50 A; A/B/C=1-239.
DR   PDB; 1PR6; X-ray; 2.10 A; A/B/C=1-239.
DR   PDB; 1PW7; X-ray; 2.00 A; A/B/C=1-239.
DR   PDBsum; 1PK7; -.
DR   PDBsum; 1PK9; -.
DR   PDBsum; 1PKE; -.
DR   PDBsum; 1PR0; -.
DR   PDBsum; 1PR1; -.
DR   PDBsum; 1PR2; -.
DR   PDBsum; 1PR4; -.
DR   PDBsum; 1PR5; -.
DR   PDBsum; 1PR6; -.
DR   PDBsum; 1PW7; -.
DR   AlphaFoldDB; P0ABP9; -.
DR   SMR; P0ABP9; -.
DR   STRING; 155864.Z5986; -.
DR   GeneID; 75202933; -.
DR   GeneID; 913500; -.
DR   KEGG; ece:Z5986; -.
DR   KEGG; ecs:ECs_5343; -.
DR   PATRIC; fig|386585.9.peg.5590; -.
DR   eggNOG; COG0813; Bacteria.
DR   HOGENOM; CLU_068457_2_0_6; -.
DR   OMA; PQCLLCG; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; Nucleoside phosphorylase domain; 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   NCBIfam; TIGR00107; deoD; 1.
DR   PANTHER; PTHR43691:SF2; PURINE NUCLEOSIDE PHOSPHORYLASE DEOD-TYPE; 1.
DR   PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS01232; PNP_UDP_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..239
FT                   /note="Purine nucleoside phosphorylase DeoD-type"
FT                   /id="PRO_0000063131"
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:0000269|PubMed:12937174"
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:0000269|PubMed:12937174"
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:0000269|PubMed:12937174"
FT   BINDING         44
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000269|PubMed:12937174"
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:0000269|PubMed:12937174"
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:0000269|PubMed:12937174"
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:0000269|PubMed:12937174"
FT   SITE            218
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT   MOD_RES         27
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           24..33
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          35..41
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           67..80
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          85..93
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          104..113
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           116..120
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           132..144
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          149..156
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           166..173
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          178..182
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           183..192
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   STRAND          196..205
FT                   /evidence="ECO:0007829|PDB:1PK9"
FT   HELIX           215..237
FT                   /evidence="ECO:0007829|PDB:1PK9"
SQ   SEQUENCE   239 AA;  25950 MW;  71D3DFAA5A176970 CRC64;
     MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLEDAREV NNVRGMLGFT GTYKGRKISV
     MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVLPHVK LRDVVIGMGA CTDSKVNRIR
     FKDHDFAAIA DFDMVRNAVD AAKALGIDAR VGNLFSADLF YSPDGEMFDV MEKYGILGVE
     MEAAGIYGVA AEFGAKALTI CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE
//