TYPH_ECOLI
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 03-AUG-2022, entry version 195.
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; Proteobacteria; 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; P07650; -.
DR PRIDE; P07650; -.
DR EnsemblBacteria; AAC77335; AAC77335; b4382.
DR EnsemblBacteria; BAE78371; BAE78371; BAE78371.
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; DVWRRMI; -.
DR PhylomeDB; P07650; -.
DR BioCyc; EcoCyc:DEOA-MON; -.
DR BioCyc; MetaCyc:DEOA-MON; -.
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:cellular response to DNA damage stimulus; 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; -; 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 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
