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Entry: A0A1M4M6K0_9FIRM
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ID   A0A1M4M6K0_9FIRM        Unreviewed;       441 AA.
AC   A0A1M4M6K0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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   Name=pdp {ECO:0000313|EMBL:SCG83336.1};
GN   ORFNames=DW1_1766 {ECO:0000313|EMBL:SCG83336.1};
OS   Proteiniborus sp. DW1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX   NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG83336.1, ECO:0000313|Proteomes:UP000185208};
RN   [1] {ECO:0000313|EMBL:SCG83336.1, ECO:0000313|Proteomes:UP000185208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW1 {ECO:0000313|EMBL:SCG83336.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-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; FMDO01000034; SCG83336.1; -; Genomic_DNA.
DR   RefSeq; WP_074350244.1; NZ_FMDO01000034.1.
DR   AlphaFoldDB; A0A1M4M6K0; -.
DR   STRING; 1889883.DW1_1766; -.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000185208; Unassembled WGS sequence.
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:SCG83336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185208};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCG83336.1}.
FT   DOMAIN          345..419
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   441 AA;  47679 MW;  D7B92DBF53B874EF CRC64;
     MRMYDIIQKK RDGKELSTEE INFFINGYSK GEIPDYQASA LLMAIYLKKM NKRETVDLTN
     AMVNSGETVD LSLIEGIKVD KHSTGGVGDK VTLALGPMVA ACGLPFAKMS GRGLGHTGGT
     LDKLESIKGL RTEFSREEFI STVNKVKLCI CSQTANITPA DKKLYALRDV TATVDNISLI
     ASSVMSKKIA AGSNAIVLDV KVGSGAFMKE LDDAFLLAEE MVGIGNSVGR ETVAIISNMD
     EPLGYAVGNS IEVIEAINTL QGNGPEDFVE LCLTLGSMLL VLGKKAENMN YGREMLVQVI
     DNGSAYNKLL EFVEAQGGDV NYIRNTELLP KASNKFEILS DCDGYIKSID AEEIGKCALA
     LGAGRETKES NIDLAAGIIL NKKVDDKVNK GDVLAYLLYN DPDKAKGIDT KLKNAIKIGD
     KNKEKKKLIY GIVDSDGVKR M
//
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