ID   TYPH_ECOLI              Reviewed;         440 AA.
AC   P07650; Q2M5T5;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 3.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Thymidine phosphorylase;
DE            EC=2.4.2.4;
DE   AltName: Full=TdRPase;
GN   Name=deoA; Synonyms=tpp, ttg; OrderedLocusNames=b4382, JW4345;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-440.
RC   STRAIN=K12;
RX   PubMed=6087276; DOI=10.1093/nar/12.13.5211;
RA   Valentin-Hansen P., Hammer K., Larsen J.E.L., Svendsen I.;
RT   "The internal regulated promoter of the deo operon of Escherichia coli K-
RT   12.";
RL   Nucleic Acids Res. 12:5211-5224(1984).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX   PubMed=6323164; DOI=10.1002/j.1460-2075.1984.tb01781.x;
RA   Valentin-Hansen P., Hammer-Jespersen K., Boetius F., Svendsen I.;
RT   "Structure and function of the intercistronic regulatory deoC-deoA element
RT   of Escherichia coli K-12.";
RL   EMBO J. 3:179-183(1984).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=2199449; DOI=10.2210/pdb1tpt/pdb;
RA   Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W.,
RA   Krenitsky T.A., Ealick S.E.;
RT   "Three-dimensional structure of thymidine phosphorylase from Escherichia
RT   coli at 2.8-A resolution.";
RL   J. Biol. Chem. 265:14016-14022(1990).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=9698549; DOI=10.1006/jmbi.1998.1941;
RA   Pugmire M.J., Cook W.J., Jasanoff A., Walter M.R., Ealick S.E.;
RT   "Structural and theoretical studies suggest domain movement produces an
RT   active conformation of thymidine phosphorylase.";
RL   J. Mol. Biol. 281:285-299(1998).
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   -!- 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   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000305}.
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DR   EMBL; U14003; AAA97278.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77335.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78371.1; -; Genomic_DNA.
DR   EMBL; X00742; CAA25324.1; -; Genomic_DNA.
DR   EMBL; X03224; CAA26975.1; -; Genomic_DNA.
DR   PIR; S56606; S56606.
DR   RefSeq; NP_418799.1; NC_000913.3.
DR   RefSeq; WP_000477807.1; NZ_LN832404.1.
DR   PDB; 1AZY; X-ray; 3.00 A; A/B=2-440.
DR   PDB; 1OTP; X-ray; 2.80 A; A=2-440.
DR   PDB; 1TPT; X-ray; 2.80 A; A=2-440.
DR   PDB; 2TPT; X-ray; 2.60 A; A=2-440.
DR   PDB; 4EAD; X-ray; 1.50 A; A=2-440.
DR   PDB; 4EAF; X-ray; 1.55 A; A=2-440.
DR   PDB; 4LHM; X-ray; 1.52 A; A=2-440.
DR   PDBsum; 1AZY; -.
DR   PDBsum; 1OTP; -.
DR   PDBsum; 1TPT; -.
DR   PDBsum; 2TPT; -.
DR   PDBsum; 4EAD; -.
DR   PDBsum; 4EAF; -.
DR   PDBsum; 4LHM; -.
DR   AlphaFoldDB; P07650; -.
DR   SMR; P07650; -.
DR   BioGRID; 4262779; 20.
DR   DIP; DIP-9426N; -.
DR   IntAct; P07650; 2.
DR   STRING; 511145.b4382; -.
DR   BindingDB; P07650; -.
DR   ChEMBL; CHEMBL3726; -.
DR   DrugBank; DB03462; Thymine.
DR   DrugCentral; P07650; -.
DR   jPOST; P07650; -.
DR   PaxDb; 511145-b4382; -.
DR   EnsemblBacteria; AAC77335; AAC77335; b4382.
DR   GeneID; 948901; -.
DR   KEGG; ecj:JW4345; -.
DR   KEGG; eco:b4382; -.
DR   PATRIC; fig|1411691.4.peg.2303; -.
DR   EchoBASE; EB0215; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_6; -.
DR   InParanoid; P07650; -.
DR   OMA; VWGGATN; -.
DR   OrthoDB; 9763887at2; -.
DR   PhylomeDB; P07650; -.
DR   BioCyc; EcoCyc:DEOA-MONOMER; -.
DR   BioCyc; MetaCyc:DEOA-MONOMER; -.
DR   BRENDA; 2.4.2.4; 2026.
DR   UniPathway; UPA00578; UER00638.
DR   EvolutionaryTrace; P07650; -.
DR   PRO; PR:P07650; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IDA:EcoCyc.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISS:CAFA.
DR   GO; GO:0046104; P:thymidine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 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   NCBIfam; TIGR02643; T_phosphoryl; 1.
DR   NCBIfam; TIGR02644; Y_phosphoryl; 1.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 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; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..440
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000059054"
FT   HELIX           4..12
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           19..30
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           36..49
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           53..64
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           94..104
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:1AZY"
FT   HELIX           123..127
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           162..171
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   TURN            172..175
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           180..192
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          197..206
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          209..213
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           214..230
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          234..241
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           253..263
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           270..286
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           293..305
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           308..319
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           326..333
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          338..343
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          349..354
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           356..365
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   TURN            366..368
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          371..375
FT                   /evidence="ECO:0007829|PDB:1OTP"
FT   STRAND          382..385
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          392..394
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          399..406
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   HELIX           407..420
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          421..426
FT                   /evidence="ECO:0007829|PDB:4EAD"
FT   STRAND          433..438
FT                   /evidence="ECO:0007829|PDB:4EAD"
SQ   SEQUENCE   440 AA;  47207 MW;  1DB3083C9275D2ED CRC64;
     MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MTMPERVSLT
     MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYIP MISGRGLGHT
     GGTLDKLESI PGFDIFPDDN RFREIIKDVG VAIIGQTSSL APADKRFYAT RDITATVDSI
     PLITASILAK KLAEGLDALV MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT
     DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL
     QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF VSEMDTRALG
     MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA VIHAKDENNW QEAAKAVKAA
     IKLADKAPES TPTVYRRISE
//