ID A0A1H8BW17_9BACI Unreviewed; 432 AA.
AC A0A1H8BW17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN ORFNames=SAMN05192533_106185 {ECO:0000313|EMBL:SEM87065.1};
OS Mesobacillus persicus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Mesobacillus.
OX NCBI_TaxID=930146 {ECO:0000313|EMBL:SEM87065.1, ECO:0000313|Proteomes:UP000198553};
RN [1] {ECO:0000313|Proteomes:UP000198553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48,IBRC-M 10115,DSM 25386,CECT 8001
RC {ECO:0000313|Proteomes:UP000198553};
RA Varghese N., Submissions S.;
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=thymidine + phosphate = 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:ARBA00048525};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine + phosphate = 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:ARBA00048453};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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; FOBW01000006; SEM87065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8BW17; -.
DR STRING; 930146.SAMN05192533_106185; -.
DR Proteomes; UP000198553; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:TreeGrafter.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR FunFam; 1.20.970.10:FF:000002; Pyrimidine-nucleoside phosphorylase; 1.
DR FunFam; 3.40.1030.10:FF:000003; Pyrimidine-nucleoside phosphorylase; 1.
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 Gene3D; 1.20.970.10; Transferase, Pyrimidine Nucleoside Phosphorylase, Chain C; 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; NF004490; PRK05820.1; 1.
DR NCBIfam; NF004747; PRK06078.1; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000198553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 343..416
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 432 AA; 45979 MW; E72AE3F8370EA7D3 CRC64;
MVDLIEKKRD GQELSTEEIQ FIINGYTDGS IPDYQVSALT MAIFFKGMTE KERADLTMAM
VKSGDQIDLS KIEGIKVDKH STGGVGDTTT LVLGPLVAAV GVPVAKMSGR GLGHTGGTID
KLEAVSGFHV EIDNEEFIQL VNKNKIAVIG QSGNLTPADK KLYALRDVTA TVDSIPLIAS
SIMSKKIAAG ADAIVLDVKT GAGAFMKTLD DSRELAKAMV QIGNNVGRNT MAVISDMSQP
LGFAIGNALE VQEAIDTLKG EGPEDLTELC LTLGSHMVYL AKKAETLKEA RALLEGAIKD
GSALESFKVF LSSQGGDASV VDDVTKLPQA KFKIELEAKE DGYVSEIVAD EIGTAAMLLG
AGRATKESQI DLAVGLVLRK KIGDKVQKGD SLLTIHSNFE DVSEVKDILY SNIRLAKDAI
EAPVLIHEEI TE
//
