TYPH_BURM7
ID TYPH_BURM7 Reviewed; 440 AA.
AC A3MAQ6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01628};
DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_01628};
DE AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_01628};
GN Name=deoA {ECO:0000255|HAMAP-Rule:MF_01628};
GN OrderedLocusNames=BMA10247_A0136;
OS Burkholderia mallei (strain NCTC 10247).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10247;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
CC -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis of
CC pyrimidine nucleosides are involved in the degradation of these
CC compounds and in their utilization as carbon and energy sources, or in
CC the rescue of pyrimidine bases for nucleotide synthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01628}.
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_01628};
CC -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC dTMP from thymine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01628}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01628}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000255|HAMAP-Rule:MF_01628}.
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DR EMBL; CP000547; ABO01892.1; -; Genomic_DNA.
DR RefSeq; WP_004188257.1; NZ_CP007801.1.
DR AlphaFoldDB; A3MAQ6; -.
DR SMR; A3MAQ6; -.
DR GeneID; 56596847; -.
DR KEGG; bmaz:BM44_3554; -.
DR KEGG; bmn:BMA10247_A0136; -.
DR PATRIC; fig|320389.8.peg.4008; -.
DR OMA; DVWRRMI; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000002284; Chromosome II.
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:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0046104; P:thymidine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1030.10; -; 1.
DR Gene3D; 3.90.1170.30; -; 1.
DR HAMAP; MF_01628; Thymid_phosp; 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 InterPro; IPR013465; Thymidine_Pase.
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 PIRSF; PIRSF000478; TP_PyNP; 1.
DR SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02643; T_phosphoryl; 1.
DR TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..440
FT /note="Thymidine phosphorylase"
FT /id="PRO_1000069656"
SQ SEQUENCE 440 AA; 45403 MW; DDC26DDD6E433A42 CRC64;
MTFLPQEFIR KVRDRAPLDT ADVARFVQGV TAGDVTEGQI AAFAMAVYFN ELPLSARIAL
TLAQRDSGDV LDWRGARLNG PVVDKHSTGG VGDLTSLVIG PMVAACGGYV PMISGRGLGH
TGGTLDKLEA IPGYDVAPSV DMLRRVVRDA GLAIVGQTAQ LAPADKRIYA VRDVTATVES
ISLITASILS KKLAAGVGAL AMDVKVGSGA FMPSAEQSAE LARSIVDVGN GAGMRTAATL
TDMNQALAPC AGNAIEVRCA IDFLTGAARP ARLEAVSFAL AAQMLTMGGL AADAHDARRR
LRAVLESGAA AERFARMVAA LGGPADLVER PERHLPRAAA AAPVAAARAG WIERIDARAL
GLAVVGLGGG RAKIGDTLDY SVGLSALAEL GERVEAGQPL ATVHARDADS AAQATDAVRR
AYRIGAEPPA QTRVVHAVIE
