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Database: UniProt
Entry: A0A0P1I9J1_9RHOB
LinkDB: A0A0P1I9J1_9RHOB
Original site: A0A0P1I9J1_9RHOB 
ID   A0A0P1I9J1_9RHOB        Unreviewed;       434 AA.
AC   A0A0P1I9J1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Thymidine phosphorylase {ECO:0000256|ARBA:ARBA00011892, ECO:0000256|HAMAP-Rule:MF_01628};
DE            EC=2.4.2.4 {ECO:0000256|ARBA:ARBA00011892, ECO:0000256|HAMAP-Rule:MF_01628};
DE   AltName: Full=TdRPase {ECO:0000256|HAMAP-Rule:MF_01628};
GN   Name=deoA {ECO:0000256|HAMAP-Rule:MF_01628,
GN   ECO:0000313|EMBL:CUJ99767.1};
GN   ORFNames=PH7735_02251 {ECO:0000313|EMBL:CUJ99767.1};
OS   Shimia thalassica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUJ99767.1, ECO:0000313|Proteomes:UP000051870};
RN   [1] {ECO:0000313|Proteomes:UP000051870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA   Rodrigo-Torres Lidia, Arahal R.David.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000749, ECO:0000256|HAMAP-
CC         Rule:MF_01628};
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01628}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01628}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|ARBA:ARBA00006915,
CC       ECO:0000256|HAMAP-Rule:MF_01628}.
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DR   EMBL; CYTW01000002; CUJ99767.1; -; Genomic_DNA.
DR   RefSeq; WP_058311435.1; NZ_CYTW01000002.1.
DR   AlphaFoldDB; A0A0P1I9J1; -.
DR   STRING; 1715693.PH7735_02251; -.
DR   GeneID; 83881276; -.
DR   UniPathway; UPA00578; UER00638.
DR   Proteomes; UP000051870; Unassembled WGS sequence.
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; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 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   NCBIfam; TIGR02644; Y_phosphoryl; 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   PIRSF; PIRSF000478; TP_PyNP; 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_01628}; Reference proteome {ECO:0000313|Proteomes:UP000051870};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01628}.
FT   DOMAIN          345..419
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   434 AA;  44881 MW;  32FB41981D9B57C0 CRC64;
     MDARAIIAAL RRGETPSQEE LTWFANGLAD GRVTDAQAGA FAMAVCLQGL GEEARVALTL
     AMRDSGDTLK WDFDGPVLDK HSTGGVGDCV SLVLAPALAA CGAYVPMISG RGLGHTGGTL
     DKMEAIPGLR TTLDEAHFRE VVRTSGCAIV SASADIAPAD KRLYAIRDVT GTVESLDLIT
     ASILSKKLAA GLQGLVLDVK VGTGAFMKTP DDALALATSL VETANLAGCP TSAVISDMNQ
     PLAPALGNAL EVAECMEVLC NGKGGALREL TVALGGVLLC NAALAPELET GIDAISKALT
     SGQAAERFGR MVAAMGGPVQ FAENWERFLP EAPVIREVLA PASGFITHMN GEALGLAVVD
     LGGGRQVQSD VVDPAVGFSD VVALGQKVVK GQPLLRIHAA REDAARRAEM AVKRAIGIGP
     VRAETPPLIH ERIR
//
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