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Database: UniProt
Entry: A0A127JXQ1_9BURK
LinkDB: A0A127JXQ1_9BURK
Original site: A0A127JXQ1_9BURK 
ID   A0A127JXQ1_9BURK        Unreviewed;       508 AA.
AC   A0A127JXQ1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Putative thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00703};
DE            EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_00703};
DE   AltName: Full=TdRPase {ECO:0000256|HAMAP-Rule:MF_00703};
GN   ORFNames=UC35_20425 {ECO:0000313|EMBL:AMO24768.1};
OS   Ramlibacter tataouinensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO24768.1, ECO:0000313|Proteomes:UP000070433};
RN   [1] {ECO:0000313|EMBL:AMO24768.1, ECO:0000313|Proteomes:UP000070433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-10 {ECO:0000313|EMBL:AMO24768.1,
RC   ECO:0000313|Proteomes:UP000070433};
RX   PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA   Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT   "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT   description of the genus Ramlibacter.";
RL   Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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:0000256|ARBA:ARBA00000749, ECO:0000256|HAMAP-
CC         Rule:MF_00703};
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. Type 2 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00703}.
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DR   EMBL; CP010951; AMO24768.1; -; Genomic_DNA.
DR   RefSeq; WP_061502964.1; NZ_CP010951.1.
DR   AlphaFoldDB; A0A127JXQ1; -.
DR   PATRIC; fig|94132.3.peg.4167; -.
DR   OrthoDB; 341217at2; -.
DR   Proteomes; UP000070433; 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; 1.20.970.50; -; 1.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 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   NCBIfam; TIGR02645; ARCH_P_rylase; 1.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 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; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00703}; Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00703}.
FT   DOMAIN          435..502
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   508 AA;  53668 MW;  118A190BE7D35FFF CRC64;
     MIEAGTVPPP NTLRLKRMGI DSYQEPVLYT RRDCHVCLSE GFEAQSRVEI SLEGRRIVAT
     LNVVDGPLLD ESEADLSEAA WRLLRAQPGD TATLRHPPPL ESLGHVRAKV YGRRLTPAAF
     DAVIADVAAG RYSDLQLAAF VTACAGERLD LEETVALTRA MVNAGERMRW SDGLVMDKHS
     VGGLPGNRTT MLIVPIVAAC GLRMPKTSSR AITSPAGTAD TMETLAPVEL DVPQIRKVVD
     AAGGCIVWGG AVRLSPADDV LIRVERPLDL DSQGQLVASV LSKKAAAGAT HVLIDMPVGP
     TAKVRSAPAA EVLARQLSLV GEALGMRVRV AHTDGSAPVG RGIGPALEAR DVLAVLRHES
     NAPGDLTQRA VHLAGELLEF GQAAREGQGA ALASAVLADG RAWRKFQQIC EAQGGMREPP
     RAPHTLPVAA ARSGSVISID NRRLARVAKL AGAPKSPCAG IDLLVQHGDF VERGQPLFVL
     HAASPGALAY AAEYARSQPD TIHVVEDA
//
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