ID   TYPH1_ACISJ             Reviewed;         511 AA.
AC   A1W631;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Putative thymidine phosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_00703};
DE            EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE   AltName: Full=TdRPase 1 {ECO:0000255|HAMAP-Rule:MF_00703};
GN   OrderedLocusNames=Ajs_1507;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 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=2.4.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00703};
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00703}.
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DR   EMBL; CP000539; ABM41706.1; -; Genomic_DNA.
DR   RefSeq; WP_011804787.1; NC_008782.1.
DR   AlphaFoldDB; A1W631; -.
DR   SMR; A1W631; -.
DR   STRING; 232721.Ajs_1507; -.
DR   EnsemblBacteria; ABM41706; ABM41706; Ajs_1507.
DR   KEGG; ajs:Ajs_1507; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_6_0_4; -.
DR   OMA; DVWRRMI; -.
DR   Proteomes; UP000000645; Chromosome.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-UniRule.
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; -; 1.
DR   Gene3D; 3.90.1170.30; -; 1.
DR   HAMAP; MF_00703; Thymid_phosp_2; 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; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR028579; Thym_Pase_Put.
DR   InterPro; IPR013466; Thymidine/AMP_Pase.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   PANTHER; PTHR10515; PTHR10515; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR02645; ARCH_P_rylase; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..511
FT                   /note="Putative thymidine phosphorylase 1"
FT                   /id="PRO_0000314694"
SQ   SEQUENCE   511 AA;  53758 MW;  4F0DA967C6F9962D CRC64;
     MSDHAMNEQR DHDTRLRAWR TGIDTYQEPI VYMRSDCVVC RSEGFTTQTR VLLTAGTRSA
     VATLNVVEGN WLAPGVAGLS EAAWHALDPA ADAWINVSYA PTLDSLSHVR AKVYGHRLDA
     GAFNAVIGDV AAGRYSDLYL AAFVTACAGD RLDLSETVAL TRAMVAVGHR LDWGRETVVD
     KHCVGGLPGN RTTLLVVPIV AACGLTMPKT SSRAITSPAG TADTMEVLAP VNLDIAAMRR
     TVERTGGCIV WGGSVRLSPA DDVLIRVERP LDLDSEGQLV ASVLSKKAAA GSTHVLIDLP
     VGPTAKVRST EAAQSLGRRL VEVGRAIGLQ VTLRITDGLQ PVGRGVGPAL EARDVLAVLR
     GQADAPDDLR QRALRLAGDI LELGGAAPNG SGLQLAAEVL ADGRAWAKFQ AICEAQGGLR
     EVPVTPYRQV ITAAVAGRVA AIDNRVLARA AKLAGAPKAP AAGVDVHARI GDPVQAGQPL
     FTLHAQTAGE LDYAGHFVDT RPPIFQISEE A