ID A0A316TPL0_9BACT Unreviewed; 448 AA.
AC A0A316TPL0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:PWN05758.1};
GN ORFNames=DDZ15_13835 {ECO:0000313|EMBL:PWN05758.1};
OS Rhodohalobacter mucosus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2079485 {ECO:0000313|EMBL:PWN05758.1, ECO:0000313|Proteomes:UP000245533};
RN [1] {ECO:0000313|EMBL:PWN05758.1, ECO:0000313|Proteomes:UP000245533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8A47 {ECO:0000313|EMBL:PWN05758.1,
RC ECO:0000313|Proteomes:UP000245533};
RA Liu Z.-W.;
RT "Rhodohalobacter halophilus gen. nov., sp. nov., a moderately halophilic
RT member of the family Balneolaceae.";
RL Submitted (MAY-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:PWN05758.1}.
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DR EMBL; QGGB01000009; PWN05758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TPL0; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000245533; Unassembled WGS sequence.
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:UP000245533};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 350..424
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 448 AA; 48404 MW; 93D6CE9640F7A729 CRC64;
MAGEKFNAVT LIRKKRDKGT LTSDEIRFLI RSYTEDSLPD YQMSAFLMAC YLNGLNTEEA
AALTKSMLHS GIVLDLNEVP GLKVDKHSTG GVGDKLSLIL APIVAACGVP VPMISGRGLG
HTGGTLDKLE SIPGFTVDMT LDRYREILKK HHLVLAGQTE DIAPADKRLY ALRDVTATVE
SIPLIAGSIM SKKLAEGIDA LVLDVKFGSG AFMKNKENAT ELARTLVNIG EEFGKETIAY
LTNMDQPLGY AVGNWLEVRE SIDALQGDGP EDVMEITHLL AGTMIYLGDK ADSVDEGVRL
SRQAVSDGSA MEKWIDIVKE QGGDAGMIMQ PESYKKADYI GNVTAQSNGY ITEMDTFALG
MVAVELGAGR REKDDSVDPA AGFMLHKKTG DTVKQGETIA VLHTNKKNML DAAGTSLLEA
ITINDSKPAP KKLITHRIDK KGVHEYAD
//