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Database: UniProt
Entry: A0A099F1Q0_9RHOB
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ID   A0A099F1Q0_9RHOB        Unreviewed;       430 AA.
AC   A0A099F1Q0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ORFNames=IT41_09635 {ECO:0000313|EMBL:KGJ04610.1}, SAMN04487972_10768
GN   {ECO:0000313|EMBL:SFA50022.1};
OS   Paracoccus halophilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ04610.1, ECO:0000313|Proteomes:UP000029846};
RN   [1] {ECO:0000313|EMBL:KGJ04610.1, ECO:0000313|Proteomes:UP000029846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04610.1,
RC   ECO:0000313|Proteomes:UP000029846};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ04610.1, ECO:0000313|Proteomes:UP000029846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04610.1,
RC   ECO:0000313|Proteomes:UP000029846};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SFA50022.1, ECO:0000313|Proteomes:UP000182312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA50022.1,
RC   ECO:0000313|Proteomes:UP000182312};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; JRKN01000010; KGJ04610.1; -; Genomic_DNA.
DR   EMBL; FOJO01000007; SFA50022.1; -; Genomic_DNA.
DR   RefSeq; WP_036740619.1; NZ_JRKN01000010.1.
DR   AlphaFoldDB; A0A099F1Q0; -.
DR   STRING; 376733.SAMN04487972_10768; -.
DR   eggNOG; COG0213; Bacteria.
DR   OrthoDB; 9763887at2; -.
DR   UniPathway; UPA00578; UER00638.
DR   Proteomes; UP000029846; Unassembled WGS sequence.
DR   Proteomes; UP000182312; 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:UP000029846};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01628}.
FT   DOMAIN          339..413
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   430 AA;  43719 MW;  0B067A18A6C0286A CRC64;
     MMAADPRPLI AAIRDGRGLD EAGAALIARG LADGTVSDAQ AAAFAMAVLL RGLDAPARVA
     LTRAMRDSGK VMHWDLPGPV VDKHSTGGIG DAVSLILAPL VAACGGFVPM ISGRGLGHTG
     GTLDKLEAIP GFRTALSEEA FRRIVAEQGC AIVAAGRDLA PADARLYAIR DESATVGSID
     LITASILSKK LAAGLDALIL DVKQGSGAFL RDERAALSLA RALVSTASGA GCRARAYITD
     MDQPLARSAG NALELREAIA VLRGERRGAL CDLSLALSSA CLGIVGISAD AARALQSGAA
     AERFARMVAA QGGPTDLLEH PDRHLPAAPV VRAVPGHGRV AAIDTEALGH AVVALGGGRL
     HARDRIDPRV GLADLLRIGE QAGPDRPLAV VHAASEGAAA AAIASVHSAY LLGDGPEPGP
     LIRDEVGLDD
//
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