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Entry: A0A0C5BFF4_9MICO
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ID   A0A0C5BFF4_9MICO        Unreviewed;       435 AA.
AC   A0A0C5BFF4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:KKM47314.1};
DE   SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:PPI13802.1};
GN   ORFNames=C5C51_08780 {ECO:0000313|EMBL:PPI13802.1}, VT73_00205
GN   {ECO:0000313|EMBL:KKM47314.1};
OS   Rathayibacter toxicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM47314.1, ECO:0000313|Proteomes:UP000052979};
RN   [1] {ECO:0000313|EMBL:KKM47314.1, ECO:0000313|Proteomes:UP000052979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FH142 {ECO:0000313|EMBL:KKM47314.1,
RC   ECO:0000313|Proteomes:UP000052979};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT   "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA 70134 or
RT   CS 32), a Western Australian isolate.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PPI13802.1, ECO:0000313|Proteomes:UP000237966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FH99 {ECO:0000313|EMBL:PPI13802.1,
RC   ECO:0000313|Proteomes:UP000237966};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-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:KKM47314.1}.
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DR   EMBL; LBFI01000001; KKM47314.1; -; Genomic_DNA.
DR   EMBL; PSWU01000013; PPI13802.1; -; Genomic_DNA.
DR   RefSeq; WP_027691762.1; NZ_PSXM01000010.1.
DR   AlphaFoldDB; A0A0C5BFF4; -.
DR   STRING; 145458.APU90_08095; -.
DR   GeneID; 66873633; -.
DR   KEGG; rtc:APU90_08095; -.
DR   KEGG; rtx:TI83_08980; -.
DR   PATRIC; fig|145458.7.peg.2047; -.
DR   eggNOG; COG0213; Bacteria.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000052979; Unassembled WGS sequence.
DR   Proteomes; UP000237966; 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:UP000052979};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          343..417
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   435 AA;  45713 MW;  588A2CECABCA93CC CRC64;
     MTTVSPVESF DAVDIIRAKR DRCTLSTAQI AWLIDAYTRG YVAGEQMAAF AMAVLLNGMD
     RDEVRDLTLA MIASGERMRF DGLGKSTVDK HSTGGVGDKI TLPLMPLVAS FGVAVPQLSG
     RGLGYTGGTL DKLESIPGWR ADLSHREILE QLRTVGGVIC AAGPGLAPAD KKLYALRDIT
     GTVEAIPLIA SSIMSKKIAE GTQALVLDVK FGSGAFLGDR DRSRELAQAM VDLGNDAGVR
     TTALLTNMNV PLGFAIGNAN EVRESVDVLA GGGPADVREL TLTLAREMLA LVGVSDADLE
     GALDDGSAMD CWRAAIRAQG GDPAAALPVA RETHVIVAER DGVLVEQQAL PFGIAAWRLG
     AGRARQCDAV QHAAGIDLHA KPGDRVRAGQ PLFTLSADEP ARFERAQEAL QGAYRIGDEG
     EEVHDGGPLV AGRIG
//
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