TYPH_RHIME
ID TYPH_RHIME Reviewed; 440 AA.
AC Q92T50;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=R00130;
GN ORFNames=SMc04122;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AL591688; CAC41517.1; -; Genomic_DNA.
DR RefSeq; NP_384236.1; NC_003047.1.
DR RefSeq; WP_010968373.1; NC_003047.1.
DR AlphaFoldDB; Q92T50; -.
DR SMR; Q92T50; -.
DR STRING; 266834.SMc04122; -.
DR EnsemblBacteria; CAC41517; CAC41517; SMc04122.
DR GeneID; 61601610; -.
DR KEGG; sme:SMc04122; -.
DR PATRIC; fig|266834.11.peg.1489; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_5; -.
DR OMA; DVWRRMI; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000001976; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..440
FT /note="Thymidine phosphorylase"
FT /id="PRO_0000059060"
SQ SEQUENCE 440 AA; 46128 MW; 9F1801BCB3A9CC3E CRC64;
MAMLPQEIIR KKRDGDRLDP AEIAGFIAGV TDGSVSEGQA AAFAMAVWFS GMNRDECVAL
TLAMRDSGET LDWSDLARPI VDKHSTGGVG DNVSLMLAPI VAACGAAVPM ISGRGLGHTG
GTLDKLESIP GYDIQPSPEL FRRVADEVGC AIIGQTADLA PADKRLYAIR DVTATVDSVP
LITASILSKK LAAGLRSLVL DVKLGNGSFM TDPAETEVLA RSLVEVANGA GVRTSALITD
MNEPLADAAG NALEIENCLA YLRGEKAGTR LDQVVMALAA EMLVAAGIAA HEAEAEAMAR
RVLGSGEAME RFGLMVHRLG GPADFVDRPG AYLAKAPAIL AVPAGRHGYL TSCKTRELGM
AVIELGGGRI RPDDRIDHRV GLTGLRPLGT KVEKGEPIAF VHAADQSQAE AIAKRVVTLY
AIADEEPARR PVIVSKLRAG
