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Entry: A0A410Q7P7_9FIRM
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ID   A0A410Q7P7_9FIRM        Unreviewed;       438 AA.
AC   A0A410Q7P7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE            EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN   ORFNames=EQM14_12460 {ECO:0000313|EMBL:QAT51331.1};
OS   Caproiciproducens sp. NJN-50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Caproiciproducens.
OX   NCBI_TaxID=2507162 {ECO:0000313|EMBL:QAT51331.1, ECO:0000313|Proteomes:UP000287564};
RN   [1] {ECO:0000313|EMBL:QAT51331.1, ECO:0000313|Proteomes:UP000287564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJN-50 {ECO:0000313|EMBL:QAT51331.1,
RC   ECO:0000313|Proteomes:UP000287564};
RA   Ma S.;
RT   "Draft genomes of a novel of Caproiciproducens strains.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides
CC       uridine, thymidine and 2'-deoxyuridine with the formation of the
CC       corresponding pyrimidine base and ribose-1-phosphate.
CC       {ECO:0000256|ARBA:ARBA00003877}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC         phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001066};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC         thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000722};
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=2.4.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001004};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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DR   EMBL; CP035283; QAT51331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410Q7P7; -.
DR   KEGG; capr:EQM14_12460; -.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000287564; Chromosome.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0047847; F:deoxyuridine phosphorylase activity; IEA:RHEA.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:RHEA.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IEA:RHEA.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   InterPro; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   NCBIfam; TIGR02644; Y_phosphoryl; 1.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:QAT51331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287564};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QAT51331.1}.
FT   DOMAIN          342..416
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   438 AA;  46876 MW;  AC288624894FB302 CRC64;
     MYDVISKKRD GGELSQTEIQ FFIDGYVKGE IPDYQASALM MAIYFKGMTA RETADLTLCM
     ARSGEMVDLS SIDGVKVDKH STGGVGDKTT LIIAPIVASL GVRVAKMSGR GLGHTGGTVD
     KMESIPGMKT SLDRETFFDI VRKVGVSVIG QSGNLVPADK KLYALRDVTA TIESIPLIAS
     SIMSKKIAAG SDCILLDVKT GSGAFMKTVD DSIRLAEAMV SIGEHVGRRT VALITDMDRP
     LGSAIGNSLE IREVCETLKG RGPQDLTAIC VELAANMLFL AGRGELPICR ELAKKQISNG
     AAFQKLREMV AAQGGDVSVL DDNSKFAQAA VRHEITSGED GFIRAMNTEE CGIASVELGA
     GREKKEDPID FSAGIVLRKK VGDRVGAGEP IAEFHTSSEQ KCREAERLFR DAVKIGAEPP
     ESIPLVHARV TKDGVEKY
//
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