ID   TYPH2_ACISJ             Reviewed;         513 AA.
AC   A1W9B0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Putative thymidine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_00703};
DE            EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE   AltName: Full=TdRPase 2 {ECO:0000255|HAMAP-Rule:MF_00703};
GN   OrderedLocusNames=Ajs_2690;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000539; ABM42835.1; -; Genomic_DNA.
DR   RefSeq; WP_011805859.1; NC_008782.1.
DR   AlphaFoldDB; A1W9B0; -.
DR   SMR; A1W9B0; -.
DR   STRING; 232721.Ajs_2690; -.
DR   EnsemblBacteria; ABM42835; ABM42835; Ajs_2690.
DR   KEGG; ajs:Ajs_2690; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_6_0_4; -.
DR   OMA; QMVASIM; -.
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..513
FT                   /note="Putative thymidine phosphorylase 2"
FT                   /id="PRO_0000314695"
SQ   SEQUENCE   513 AA;  53719 MW;  EEA4E3707AC03BAE CRC64;
     MTAQMHEAGR TKEAGNRLQA WRTGIDTYQE PVVYMRRDCP VCRSEGFTTQ ARVQLTAGGR
     SIVATLSVVD GDWLAENVAG LSESAWASLG AQPGEPVAVT HAPPLDSLSH VRAKVYGNSL
     GDAQFGAIIS DVAAGRYSDL HLATFITACA GDRLDLAETL SLTKAMIAVG DRIDWGRPLV
     VDKHCVGGLP GNRTTLLVVP IVTACGLMMP KTSSRAITSP AGTADTMEVL APVNLDVPSM
     RRVVERTGGC IVWGGSVRLS PADDILIRVE RPLDLDSEGQ LVASVLSKKA AAGSTHVLID
     LPVGATAKVR SAHAAASLGR RLQEVGGAIG LQVFLRVTDG EQPVGRGIGP ALEARDVLAV
     LQGTREAPAD LRERALRLAA DILEMGGAAP AGGGLKLATE VLADGRAWAK FQAICSEQGG
     LRSLPMAAHL HTVESPGTGR VTRIDNRLLA RAAKLAGAPT APAAGIDVHA RLGDRVEAGQ
     PLFTLHAQAP GELAYALEFV RARPPIFQIS ENV