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Database: UniProt
Entry: A6LY31_CLOB8
LinkDB: A6LY31_CLOB8
Original site: A6LY31_CLOB8 
ID   A6LY31_CLOB8            Unreviewed;       237 AA.
AC   A6LY31;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 98.
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   OrderedLocusNames=Cbei_3125 {ECO:0000313|EMBL:ABR35261.1};
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR35261.1, ECO:0000313|Proteomes:UP000000565};
RN   [1] {ECO:0000313|EMBL:ABR35261.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR35261.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=21962126; DOI=10.1186/1471-2164-12-479;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Single-nucleotide resolution analysis of the transcriptome structure of
RT   Clostridium beijerinckii NCIMB 8052 using RNA-Seq.";
RL   BMC Genomics 12:479-479(2011).
RN   [3] {ECO:0000313|EMBL:ABR35261.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=22433311; DOI=10.1186/1471-2164-13-102;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Genome-wide dynamic transcriptional profiling in clostridium beijerinckii
RT   NCIMB 8052 using single-nucleotide resolution RNA-Seq.";
RL   BMC Genomics 13:102-102(2012).
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|ARBA:ARBA00010456, ECO:0000256|HAMAP-Rule:MF_01627}.
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DR   EMBL; CP000721; ABR35261.1; -; Genomic_DNA.
DR   RefSeq; WP_012059312.1; NC_009617.1.
DR   AlphaFoldDB; A6LY31; -.
DR   KEGG; cbe:Cbei_3125; -.
DR   eggNOG; COG0813; Bacteria.
DR   HOGENOM; CLU_068457_2_0_9; -.
DR   OMA; CSIYVHE; -.
DR   Proteomes; UP000000565; Chromosome.
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: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.
DR   PROSITE; PS01232; PNP_UDP_1; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01627};
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   237 AA;  25441 MW;  563D7E3DEBBD2D0B CRC64;
     MTNVPTPHNG AKLGEIAKTV LMPGDPLRAK FIAENFLEDV TQFNTVRNML GYTGTYKGKR
     VSVMGGGMGM PSIGIYSYEL FNFYGVDNII RIGTAGSISE KLHLRDVVIG LGASTNSNYA
     HQYNLPGTFA PIASFDLVSS AVEAAKENNI NVVVGNILSS DTFYSADKTA TEKWKSMGVL
     AIEMEAAALY MNAAEAGKNA LCLLTISDSV LTGESLSAED RQLSFTEMMK IALEIAK
//
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