ID A0A1H1SNY3_9ACTN Unreviewed; 429 AA.
AC A0A1H1SNY3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:SDS49109.1};
GN ORFNames=SAMN04489717_2862 {ECO:0000313|EMBL:SDS49109.1};
OS Actinopolymorpha singaporensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Actinopolymorphaceae; Actinopolymorpha.
OX NCBI_TaxID=117157 {ECO:0000313|EMBL:SDS49109.1, ECO:0000313|Proteomes:UP000198983};
RN [1] {ECO:0000313|EMBL:SDS49109.1, ECO:0000313|Proteomes:UP000198983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22024 {ECO:0000313|EMBL:SDS49109.1,
RC ECO:0000313|Proteomes:UP000198983};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; LT629732; SDS49109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1SNY3; -.
DR STRING; 117157.SAMN04489717_2862; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000198983; Chromosome i.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000198983};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 339..413
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 429 AA; 44534 MW; EE0F85703B327D92 CRC64;
MTEHFDAVDV IRAKRDGHRL TDAQIDWVVD AYTRGAVADE QMSALLMAVL LRGMESAEIA
RWTRAMISSG ERLDFAGVGR PTADKHSTGG VGDKITLPLA AVVAACGVAV PQLSGRGLGH
TGGTLDKLES IPGWRASLSY DEIVVQLRDV GAVICAPTDT LAPADRKLYA LRDVTGTVES
IPLIASSIMS KKIAEGTGAL VLDVKVGSGA FMKNAEDARA LAATMVELGR SAGVRTVALL
TDMTTPLGLT AGNALEVRES VEVLAGGGPR DVVELTVALA REMLTAAGAA GGPDPSDVLK
DGTAMDVWRS MIRAQGGDPD APLPRAAHTH EVPAPAEGVL VRLDAYQVGV AAWRLGAGRS
RKEDPVSAGA GVEMHAKPGA LVRAGQPLLT LHADDPARFA RALEALEGAV EIAPKGAGTD
QKLILGRIE
//