TYPH2_CUPPJ
ID TYPH2_CUPPJ Reviewed; 512 AA.
AC Q46S32;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative thymidine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_00703};
DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE AltName: Full=TdRPase 2 {ECO:0000255|HAMAP-Rule:MF_00703};
GN OrderedLocusNames=Reut_B4704;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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_00703};
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00703}.
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DR EMBL; CP000091; AAZ64052.1; -; Genomic_DNA.
DR RefSeq; WP_011300818.1; NC_007348.1.
DR AlphaFoldDB; Q46S32; -.
DR SMR; Q46S32; -.
DR STRING; 264198.Reut_B4704; -.
DR EnsemblBacteria; AAZ64052; AAZ64052; Reut_B4704.
DR KEGG; reu:Reut_B4704; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_4; -.
DR OMA; CSTHTDY; -.
DR OrthoDB; 1724909at2; -.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan 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:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 3.40.1030.10; -; 1.
DR Gene3D; 3.90.1170.30; -; 1.
DR HAMAP; MF_00703; Thymid_phosp_2; 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; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR028579; Thym_Pase_Put.
DR InterPro; IPR013466; Thymidine/AMP_Pase.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
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 SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02645; ARCH_P_rylase; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..512
FT /note="Putative thymidine phosphorylase 2"
FT /id="PRO_0000314711"
SQ SEQUENCE 512 AA; 53921 MW; 8CCDB5A89B7907E7 CRC64;
MQANELKLAA GEGQGSEPLI FKPLGIDTWQ EHVIYLHPDC PVCRAEGFTA QARVQVRIGE
ASLIATLNLV GAPLLDTGEA SLSASAAQAL EARAGDVVAI SHAPALESVR ALRAKIYGRR
LDGAQIDSII SDISAGRYPD VYISAFLAAC ADGRMNRRET VDLTRAMVHS GERLSWSHAV
VADKHCVGGL PGNRTTPIVV AIAAAGGLVL PKTSSRAITS PAGTADTMET LTRVALSAAE
LRHVVERVGA SLVWGGALNL SPADDILIRV ERALDIDSDA QLVASILSKK VAAGSTHILI
DVPVGPTAKV REDRDLERLE AAMRHVAGAF GLHILMVRTD GTQPLGRGIG PALEARDILA
VLQRTVAAPP DLRERSVMLA GALLEFCGAA PRGAGEKAAG QLLDSGAAWR KFQAICEAQG
GLRVPGEAIF RRDIVAPHAG KVIAIDNRHI ARTAKLAGAP MRQVAGLEMR VRVNDEVRAG
QPLFTVHAQA SGELDYSCSY ALAHPAVSIE PH