TYPH_PARL1
ID TYPH_PARL1 Reviewed; 505 AA.
AC A7HYS8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Putative thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_00703};
DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_00703};
GN OrderedLocusNames=Plav_3461;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS65061.1; -; Genomic_DNA.
DR RefSeq; WP_012112373.1; NC_009719.1.
DR AlphaFoldDB; A7HYS8; -.
DR SMR; A7HYS8; -.
DR STRING; 402881.Plav_3461; -.
DR EnsemblBacteria; ABS65061; ABS65061; Plav_3461.
DR KEGG; pla:Plav_3461; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR OMA; DVWRRMI; -.
DR OrthoDB; 1724909at2; -.
DR Proteomes; UP000006377; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..505
FT /note="Putative thymidine phosphorylase"
FT /id="PRO_0000314705"
SQ SEQUENCE 505 AA; 54109 MW; 703494434635F8A3 CRC64;
MSARITPQTP ALQALRMRLH AQHQPVVLMR TDCHVCRAEG LAPRSQVLII AGDRTVQALL
YQIDSDLLKT GQIALSEAAW DALDIHEGDL VQVRHPPLLE SLSAVRARIH GHRLQTTELQ
AIVRDVVDGR YTDVALSAFL TATAVLPLDM QETIHLTRAM VDVGDHLQWQ APIVVDKHCV
GGLPGNRTTP LVVAIAAANG LVMPKTSSRA ITSPAGTADT METLAPVDLD LDTLRKVVEK
EGGCVAWGGA MHLSPADDIF VRIERELDID TQGQLIASVL SKKIAAGATH IVIDIPVGPT
AKVRSRETAE HLAHHLSEVA ASFGLVLRCL FTDGNQPVGR GIGPALEARD VLAVLRNEAD
APQDLCDRVA LVAGAVLELG GVAKEGDGIR LAHETISSGR AWEKFQRICA AQGGFREPPQ
ALYVEPLLAT TSGRAVHIDN RKLSRLAKLA GAPESPAAGI QLQVRLGDEV TRGQSLMFLH
AQTSGEMAYA LAYVHDIGDI VKIEP