ID A0A2A9CJ39_9BACI Unreviewed; 433 AA.
AC A0A2A9CJ39;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN ORFNames=ATG70_1916 {ECO:0000313|EMBL:PFG13700.1};
OS Bacillus sp. es.036.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761764 {ECO:0000313|EMBL:PFG13700.1, ECO:0000313|Proteomes:UP000222003};
RN [1] {ECO:0000313|EMBL:PFG13700.1, ECO:0000313|Proteomes:UP000222003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=es.036 {ECO:0000313|Proteomes:UP000222003};
RA Fredrickson J.;
RT "Microbial Interactions in Extremophilic Mat Communities.";
RL Submitted (OCT-2017) 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:PFG13700.1}.
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DR EMBL; PDIZ01000001; PFG13700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9CJ39; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000222003; Unassembled WGS sequence.
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: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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..418
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 433 AA; 46554 MW; ED6DDE0C9E6690FC CRC64;
MRMVDVIQKK RNGKELTKEE INFFIEGYTK GDIPDYQASA LMMAIYFNGM KSNETALLTQ
AMVESGETID LSAIKGHKVD KHSTGGVGDK TTFIVGPLVA SVGVPVAKMS GRGLGHTGGT
LDKLESIKGF HIEMTKEEFV SNVNTHKLSV AGQTGNLAPA DKKLYALRDV TATVDSIPLI
AGSIMSKKLA SGADGIVLDV KTGSGAFMKK LEDSEALARE MVNIGNNLGR NTVAVISDMS
QPLGFEVGNA NEVREACQVL QGENIEDLRL LSLELASHMT VIAGAFDDFE TAYKTLEENL
QNGKAFESFR TLVQAQGGDV SVIDDLSKLP QAKHDIEVTA QQDGYVTEID AESVGVAAMY
LGAGRATKDD QINHGVGITL KKKVGDKVEK GEALVVLHSD EEDVQNSINK INEAYTVSKQ
ATEKPQLIYK VIN
//
