TYPH_TOLAT
ID TYPH_TOLAT Reviewed; 505 AA.
AC C4LAA1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Putative thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_00703};
DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_00703};
GN OrderedLocusNames=Tola_2482;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) 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; CP001616; ACQ94076.1; -; Genomic_DNA.
DR RefSeq; WP_015879528.1; NC_012691.1.
DR AlphaFoldDB; C4LAA1; -.
DR SMR; C4LAA1; -.
DR STRING; 595494.Tola_2482; -.
DR EnsemblBacteria; ACQ94076; ACQ94076; Tola_2482.
DR KEGG; tau:Tola_2482; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_6; -.
DR OMA; CSTHTDY; -.
DR OrthoDB; 1724909at2; -.
DR Proteomes; UP000009073; 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..505
FT /note="Putative thymidine phosphorylase"
FT /id="PRO_1000212645"
SQ SEQUENCE 505 AA; 54040 MW; 5FE1A9E834782093 CRC64;
MSARITPQTP ALQALRMRLH AQHQPVVLMR TDCHVCRAEG LAPRSQVLII AGDRTVQALL
YQIDSDLLKT GQIALSEAAW DALDIHEGDL VQVRHPPLLE SLSAVRARIH GHRLQTTELQ
AIVRDVVDGR YTDVALSAFL TATAVLPLDM QETIHLTRAM VDVGDHLQWQ APIVVDKHCV
GGLPGNRTTP LVVAIAAANG LVMPKTSSRA ITSPAGTADT METLAPVDLD LDTLRKVVEK
EGGCVAWGGA MHLSPADDIF VRIERELDID TQGQLIASVL SKKIAAGATH IVIDIPVGPT
AKVRSRETAE HLAHHLSEVA ASFGLVLRCL FTDGNQPVGR GIGPALEARD VLAVLRNEAD
APQDLCDRVA LVAGAVLELG GVAKEGDGIR LAHETISSGR AWEKFQRICA AQGGFREPPQ
ALYVEPLLAT TTGRAVHIDN RKLSRLAKLA GAPESSAAGI QLQVRLGDEV TSGQPLMFLH
AQTSGEMAYA LAYVHDIGDI VNIEP