ID A0A1I1NSC2_9CLOT Unreviewed; 434 AA.
AC A0A1I1NSC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN ORFNames=SAMN05421842_11674 {ECO:0000313|EMBL:SFD00564.1};
OS Clostridium uliginosum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=119641 {ECO:0000313|EMBL:SFD00564.1, ECO:0000313|Proteomes:UP000199263};
RN [1] {ECO:0000313|EMBL:SFD00564.1, ECO:0000313|Proteomes:UP000199263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12992 {ECO:0000313|EMBL:SFD00564.1,
RC ECO:0000313|Proteomes:UP000199263};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOMG01000016; SFD00564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1NSC2; -.
DR STRING; 119641.SAMN05421842_11674; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000199263; Unassembled WGS sequence.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000199263};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 434 AA; 46785 MW; 25C854083AA6565F CRC64;
MKMIDIINKK RMGMELSTEE INFFIQNYTN GSIPDYQVSA LLMAIYFQKM NMRETSDLTM
AMVNSGDVLD LSNIEGIKVD KHSTGGVGDT TSLVLTPMVA SLGIPVAKMS GRGLGHTGGT
IDKLESFDGF SVEISEEQFI NNVNKDKIAI MGQTADLAPA DKKLYALRDV TGTVQNISLI
SSSIMSKKIA SGADAIVLDV KVGDGAFMKT FENAKELATA MVSIGKNVGR NTVAVISDMD
QPLGLAVGNA LEVKEAIDTL KGNGPDDLLE LCLTLGSNMV VLAKKAETVE EARKMLLKVI
EDGSALRKLK EFIAAQGGNP EQVENPELLP KAKYVVEVKS EVEGYVSKID SEHIGLIAME
LGAGRATKED KIDLAVGIVL NKKRSDKVSK GETLAYIHAN DESKIEKAGK DIIVSYHILN
ENRKAVPLIY GVVK
//
