ID A0A135WB59_9BACL Unreviewed; 433 AA.
AC A0A135WB59;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 18-JUN-2025, entry version 36.
DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680};
DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889};
GN Name=deoA {ECO:0000313|EMBL:KXH82111.1};
GN ORFNames=AU377_07370 {ECO:0000313|EMBL:KXH82111.1};
OS Sporosarcina sp. HYO08.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC Sporosarcina.
OX NCBI_TaxID=1759557 {ECO:0000313|EMBL:KXH82111.1, ECO:0000313|Proteomes:UP000070230};
RN [1] {ECO:0000313|EMBL:KXH82111.1, ECO:0000313|Proteomes:UP000070230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYO08 {ECO:0000313|EMBL:KXH82111.1,
RC ECO:0000313|Proteomes:UP000070230};
RA Choi I.-G., Park W.;
RT "Draft genome sequences of microorganisms having biocementation activity.";
RL Submitted (DEC-2015) 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}.
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:KXH82111.1}.
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DR EMBL; LPUT01000023; KXH82111.1; -; Genomic_DNA.
DR RefSeq; WP_067407274.1; NZ_LPUT01000023.1.
DR AlphaFoldDB; A0A135WB59; -.
DR STRING; 1759557.AU377_07370; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000070230; 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: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; 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 Reference proteome {ECO:0000313|Proteomes:UP000070230};
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 433 AA; 45589 MW; D5BD5D0C0256CA89 CRC64;
MVDIIEKKRN GGQLTEQEIT FFVNGYTNGT IPDYQASAFL MAVYFKGMTA EEQGHLTMAM
VKSGDEIDLS AIRGIKVDKH STGGVGDTTT LILAPLVAAC GVPVAKMSGR GLGHTGGTLD
KLESIGGFHV ELTEEQFINQ VNELKVAVIG QSGNLTPADK SLYALRDVTA TVDSIPLIAS
SIMSKKIAAG ADAIVLDVKT GEGAFMKTVE DAKALAESMV AIGRQVGRNT MAVISNMSQP
LGFAIGNALE VKEAIETLKG EGPEDLTELC LVLGSKMLVV GGKAETIEEA RGQLTAVMKD
GSALKLFGEL IKAQGGNEAV IHDPSKLPTA TYQIEVPALQ SGFITKMEAD DLGVAAAILG
AGRATKDDQI DPAVGIMLKK KIGDTVEKGE TIAIIHSNSK EIEKSLQLLQ EHIRIENDYV
APPSLIGDVI TGD
//
