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Entry: A0A2P8E1E0_9ACTN
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ID   A0A2P8E1E0_9ACTN        Unreviewed;       436 AA.
AC   A0A2P8E1E0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:PSL03217.1};
GN   ORFNames=CLV30_108129 {ECO:0000313|EMBL:PSL03217.1};
OS   Haloactinopolyspora alba.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Jiangellales;
OC   Jiangellaceae; Haloactinopolyspora.
OX   NCBI_TaxID=648780 {ECO:0000313|EMBL:PSL03217.1, ECO:0000313|Proteomes:UP000243528};
RN   [1] {ECO:0000313|EMBL:PSL03217.1, ECO:0000313|Proteomes:UP000243528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45211 {ECO:0000313|EMBL:PSL03217.1,
RC   ECO:0000313|Proteomes:UP000243528};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSL03217.1}.
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DR   EMBL; PYGE01000008; PSL03217.1; -; Genomic_DNA.
DR   RefSeq; WP_106537623.1; NZ_ML142902.1.
DR   AlphaFoldDB; A0A2P8E1E0; -.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000243528; 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; 1.20.970.10:FF:000004; Thymidine phosphorylase; 1.
DR   FunFam; 3.40.1030.10:FF:000001; Thymidine 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000243528};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          345..419
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   436 AA;  45359 MW;  561C4A15EC66D279 CRC64;
     MNDAASGTEP FDVVDVIRAK RDHAELPDAQ IDWVVDAYTR GIVADEQMSA LAMAILLNGM
     SRREIARWTE AMIGTGRRMD WSGVQRPTTD KHSTGGVGDK ITLPLAPTVA ACGAAVPQLS
     GRGLGHTGGT LDKLESIPGW RASLSPDEML SVLRDTGAVV CAAGADLAPA DKRLYALRDV
     TGTVESIPLI ASSIMSKKIA EGTAALVLDV KVGSGAFMKD VESARELAET MVALGTDAGV
     RTVALLTNMA TPLGLTAGNA LEVAEAVEVL GGGGPDDVVE LTVRLAREML EVSGQGGAKD
     PADALRDGTA MDVWRRMIAG QGGDPDADLP RARETHTILA PADGTLASLD AYQVGVAAWR
     LGAGRGRQDE PVQAAAGVRM HVKPGAVVRS GEPLLTLHTD EPARIQRAVD ALDGAYVIAP
     AGSRPDLLPL VVDRVS
//
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