TYPH_AERS4
ID TYPH_AERS4 Reviewed; 443 AA.
AC A4SRU3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=ASA_3654;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO91615.1; -; Genomic_DNA.
DR RefSeq; WP_005320414.1; NC_009348.1.
DR AlphaFoldDB; A4SRU3; -.
DR SMR; A4SRU3; -.
DR STRING; 382245.ASA_3654; -.
DR EnsemblBacteria; ABO91615; ABO91615; ASA_3654.
DR KEGG; asa:ASA_3654; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_6; -.
DR OMA; DVWRRMI; -.
DR OrthoDB; 1724909at2; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000000225; 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; Transferase.
FT CHAIN 1..443
FT /note="Thymidine phosphorylase"
FT /id="PRO_1000069655"
SQ SEQUENCE 443 AA; 46920 MW; 5E92E37014707542 CRC64;
MFLPQEIIRK KRNGEALSTQ EIQFFVQGIT NNTIGEGQIA ALAMAVYFKD MTMDERVALT
CAMRDSGMVL NWEHLNLGGP IVDKHSTGGV GDVVSLMLGP MVAACGGFVP MISGRGLGHT
GGTLDKLDAI PGYQTSVDND RFLKVVKEAG VAIIGQTGDL APADKRIYAV RDITATVESI
AMITGSILSK KLASGLEALV MDVKVGSGAF MPTFEASEEL AKSIVAVANG AGCRTSALLT
DMNQVLASSA GNGVEVREAV RYLTGEYRNP RIHEVTMSLC AEMLISAHLA SDDADARRKL
QAVLDNGKAA EIFGRMVTGL GGPSDFMERY DSYLPKAAIV RPVYAANAGF VTAMDTRELG
LAVVAMGGGR RAAGDKLDYA VGLTDFIRLG QSVDADKPLA LIHAQTEDQF AQAASMVQAA
VKIGDTQPQA LPEVYRRIGL ADL
