ID   A0A239PXJ4_9RHOB        Unreviewed;       429 AA.
AC   A0A239PXJ4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=thymidine phosphorylase {ECO:0000256|ARBA:ARBA00011892};
DE            EC=2.4.2.4 {ECO:0000256|ARBA:ARBA00011892};
GN   ORFNames=SAMN05444959_108102 {ECO:0000313|EMBL:SNT74662.1};
OS   Paracoccus seriniphilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=184748 {ECO:0000313|EMBL:SNT74662.1, ECO:0000313|Proteomes:UP000198307};
RN   [1] {ECO:0000313|EMBL:SNT74662.1, ECO:0000313|Proteomes:UP000198307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14827 {ECO:0000313|EMBL:SNT74662.1,
RC   ECO:0000313|Proteomes:UP000198307};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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DR   EMBL; FZQB01000008; SNT74662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239PXJ4; -.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000198307; 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-EC.
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; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198307};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          338..412
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   429 AA;  44353 MW;  471CD47314A509F8 CRC64;
     MTDPRPVIAA IRDGRRLDGP GAALIAQGLA NGSVSDAQAG AFAMAVLIRG LDEEGRVALT
     RAMRDSGQLM RWDLPGPVVD KHSTGGIGDT VSLILAPLLA ARGVYVPMIS GRGLGHTGGT
     LDKLEAIPGF LCDQSQEQLQ TIVGNIGCAI VSATGDIAPA DRRLYAIRDE SGTVESLDLI
     TASILSKKLA AGLDALVLDV KEGSGALLRK GNSTRALAEA LVRTANGAGC RCSAFVTDMD
     QPLAQSAGNA LEVAEAIAVL RGKKGALRDL TLALAREVLA LAGQGTEGLD ETLESGAAAE
     RFSRMIAAQG GPADLLERPE AYLARAPVVR PVPAPSGKVS KIDVTALGHV VVALGGGRTR
     AGEQIDHRVG LDRMARLGDE VGHENPLGFV HAADDVGAEI AIRAVQDAYQ IAQDAQSGPL
     IRHRVDADE
//