TYPH_SALTY
ID TYPH_SALTY Reviewed; 440 AA.
AC Q7CP66;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=STM4568;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL23383.1; -; Genomic_DNA.
DR RefSeq; NP_463424.1; NC_003197.2.
DR RefSeq; WP_000477838.1; NC_003197.2.
DR PDB; 4X46; X-ray; 2.20 A; A/B=1-440.
DR PDB; 4XR5; X-ray; 2.05 A; A/B=1-440.
DR PDB; 4YEK; X-ray; 2.55 A; A/B=1-440.
DR PDB; 4YYY; X-ray; 2.43 A; A/B=1-440.
DR PDB; 5EY3; X-ray; 1.91 A; A/B=1-440.
DR PDBsum; 4X46; -.
DR PDBsum; 4XR5; -.
DR PDBsum; 4YEK; -.
DR PDBsum; 4YYY; -.
DR PDBsum; 5EY3; -.
DR AlphaFoldDB; Q7CP66; -.
DR SMR; Q7CP66; -.
DR STRING; 99287.STM4568; -.
DR PaxDb; Q7CP66; -.
DR EnsemblBacteria; AAL23383; AAL23383; STM4568.
DR GeneID; 1256094; -.
DR KEGG; stm:STM4568; -.
DR PATRIC; fig|99287.12.peg.4810; -.
DR HOGENOM; CLU_025040_0_1_6; -.
DR OMA; DVWRRMI; -.
DR PhylomeDB; Q7CP66; -.
DR BioCyc; SENT99287:STM4568-MON; -.
DR BRENDA; 2.4.2.4; 5542.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..440
FT /note="Thymidine phosphorylase"
FT /id="PRO_0000059064"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4X46"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:5EY3"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 214..230
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 270..286
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4YEK"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:5EY3"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:4XR5"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4YYY"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:5EY3"
FT HELIX 407..420
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:5EY3"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:5EY3"
SQ SEQUENCE 440 AA; 47002 MW; CF534028471AD475 CRC64;
MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MTMPERVSLT
MAMRDSGTVL DWKSLNLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYVP MISGRGLGHT
GGTLDKLEAI PGFDIFPDDN RFREIIQDVG VAIIGQTSSL APADKRFYAT RDITATVDSI
PLITGSILAK KLAEGLDALV MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT
DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGQLA KDDAEARAKL
QAVLDNGKAA EVFGRMVAAQ KGPSDFVENY DKYLPTAMLS KAVYADTEGF ISAMDTRALG
MAVVSMGGGR RQASDTIDYS VGFTDMARLG DSIDGQRPLA VIHAKDEASW QEAAKAVKAA
IILDDKAPAS TPSVYRRITE
