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Database: UniProt
Entry: U4TRV5_9LACO
LinkDB: U4TRV5_9LACO
Original site: U4TRV5_9LACO 
ID   U4TRV5_9LACO            Unreviewed;       430 AA.
AC   U4TRV5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE            EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN   ORFNames=L248_0690 {ECO:0000313|EMBL:ERL64633.1};
OS   Schleiferilactobacillus shenzhenensis LY-73.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL64633.1, ECO:0000313|Proteomes:UP000030647};
RN   [1] {ECO:0000313|Proteomes:UP000030647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX   PubMed=24265500;
RA   Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA   Yang R., Liu F.;
RT   "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL   Genome Announc. 1:e00972-e00913(2013).
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   -!- 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; KI271594; ERL64633.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4TRV5; -.
DR   STRING; 1231336.L248_0690; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_9; -.
DR   Proteomes; UP000030647; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          343..416
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   430 AA;  44944 MW;  6CD2B081B5B2A6C1 CRC64;
     MVDIIQAKRD GRELTKEQIQ FVISGYTAGT IPDYQMSALL MAIYFEDMTP LEIGALTDAM
     LHSGDVLDLS AIPGIKVDKH STGGVGDKIS IPLAPLVAAA GAKNPMISGR GLGHTGGTLD
     KLEAIPGFNV DLTEQQFIDQ VTTVGTAITS ATGNLAPADK KIYALRDVTG TVEAIPLISS
     SIMSKKLASG TDGLVLDVKT GNGAFMKTEE RAAALARALV RIGHLAGIKI IALLTDMDQP
     LGFTIGNALE IQESIAILQN QGPADVRDLT LTLGSHMLLQ ANLADDLTGA RHILEKHLAD
     GSALAKFKEM ITAQGGDAGV VDDPTKLPQA KHTIPVLSTE AGMVTGMATD QLGVASMILG
     GGRQKKGDAI DPAVGIMLHK KIGDRVANGE LLATIYAEEA QRPDVQAMVS EAIHLGPTAT
     VPPLVHQVIE
//
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