ID A0A3A1V0S6_9BACL Unreviewed; 443 AA.
AC A0A3A1V0S6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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=D3P08_08270 {ECO:0000313|EMBL:RIX53426.1};
OS Paenibacillus nanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=393251 {ECO:0000313|EMBL:RIX53426.1, ECO:0000313|Proteomes:UP000266482};
RN [1] {ECO:0000313|EMBL:RIX53426.1, ECO:0000313|Proteomes:UP000266482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22867 {ECO:0000313|EMBL:RIX53426.1,
RC ECO:0000313|Proteomes:UP000266482};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA Laiz L., Saiz-Jimenez C.;
RT "Paenibacillus aracenensis nov. sp. isolated from a cave in southern
RT Spain.";
RL Submitted (SEP-2018) 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIX53426.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QXQA01000004; RIX53426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1V0S6; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000266482; 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:RIX53426.1}; Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000266482};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RIX53426.1}.
FT DOMAIN 345..420
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 443 AA; 46661 MW; 93EEBBDBDD994327 CRC64;
MRAVDLIQKK RDGGELTPEE LKFLIHGYSR GEVPDYQMSA FAMAVFFKGM TASETAALTM
SMAESGDQVD LSPIHGVKVD KHSTGGVGDK TTLIIGPLVA SVGVPVAKMS GRGLGHTGGT
IDKLESIRGF HTELTRDAFM KQVNDIGLSV IGQSSDLAPA DKKLYALRDV TGTVESIPLI
ASSVMSKKIA AGADAIVLDV KTGSGAFMKT VQDAEALAQA MVSIGTNVGR RTAAVISDMD
QPLGYAIGNA LEVAEALDTL RGQGPEDLTE LCLTLGAHMV TLGGKARTFD EAKSKLRKQL
ENGEALAKFK AFIEAQGGDG GIVDQPDKLP QAPFAVEVTA DAEGYISAIQ AEQLGLAAML
LGAGRATKEA VIDYAVGLTL RKKVGDTVQA GDTLAILHVR DNNDAARQVA DRVRGAYIIQ
TERPETRPLL LSVVTADGIE RFI
//
