TYPH_SPHAL
ID TYPH_SPHAL Reviewed; 514 AA.
AC Q1GQ92;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Sala_2473;
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF54180.1; -; Genomic_DNA.
DR RefSeq; WP_011542745.1; NC_008048.1.
DR AlphaFoldDB; Q1GQ92; -.
DR SMR; Q1GQ92; -.
DR STRING; 317655.Sala_2473; -.
DR EnsemblBacteria; ABF54180; ABF54180; Sala_2473.
DR KEGG; sal:Sala_2473; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR OMA; DVWRRMI; -.
DR OrthoDB; 1724909at2; -.
DR Proteomes; UP000006578; 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..514
FT /note="Putative thymidine phosphorylase"
FT /id="PRO_0000314718"
SQ SEQUENCE 514 AA; 52830 MW; 7FB57264EA8DACDA CRC64;
MTHPVPDTGP ASENMAPHRL RARPLGLFLP QQQPAVVMRT DCYICRSEGL AARSQVLIQA
GGREILASLL HSSGEMIAPG EIGLSESAAA ALGVAPGDAV SVRHAPPIDS FGALRGRVYG
NRLDGAAFRS IVDDIVAGRY SDVHLSAFVT ACSAFPLDHA ETVALTGAMV ASGERLAWGS
DVVVDKHSVG GLPGNRTTPI VVAIVAALGL IMPKTSSRAI TSPAGTADTM ETLAPVNLDV
GAIRRVVDHE GGCIVWGGAV SLSPADDIII GVERVLDLDA AGQLVASVLS KKLAAGATHL
VVDMPIGPTA KVRSPADAAA LSGALQKVAA EFGLILKVMQ GDGREPIGRG IGPALEARDI
LAVLEGRDPP PDLARRACEL AGALIELAGR ASPGTGAALA AQVLADGSAW SKFQRICEAQ
GGMRTPPLSN HRHVMTAQRP GRVSAIDNRR LAKLAKLAGA PAAKSAGLEM HVRLGSAVET
GTPLLTVHAE SQGELAYALA YAEAVGPILE LSDR