ID I3KNP0_ORENI Unreviewed; 471 AA.
AC I3KNP0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Thymidine phosphorylase {ECO:0000256|PIRNR:PIRNR000478};
DE Short=TP {ECO:0000256|PIRNR:PIRNR000478};
DE EC=2.4.2.4 {ECO:0000256|PIRNR:PIRNR000478};
DE AltName: Full=TdRPase {ECO:0000256|PIRNR:PIRNR000478};
GN Name=TYMP {ECO:0000313|Ensembl:ENSONIP00000022735.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000022735.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000022735.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The
CC produced molecules are then utilized as carbon and energy sources or in
CC the rescue of pyrimidine bases for nucleotide synthesis.
CC {ECO:0000256|PIRNR:PIRNR000478}.
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|PIRNR:PIRNR000478};
CC -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC dTMP from thymine: step 1/2. {ECO:0000256|PIRNR:PIRNR000478}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000478}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915,
CC ECO:0000256|PIRNR:PIRNR000478}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; I3KNP0; -.
DR STRING; 8128.ENSONIP00000077763; -.
DR Ensembl; ENSONIT00000022755.2; ENSONIP00000022735.2; ENSONIG00000018041.2.
DR eggNOG; ENOG502QPRY; Eukaryota.
DR GeneTree; ENSGT00390000009250; -.
DR HOGENOM; CLU_025040_0_2_1; -.
DR TreeFam; TF332198; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000005207; Linkage group LG17.
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:0006213; P:pyrimidine nucleoside 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 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 ECO:0000256|PIRNR:PIRNR000478};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000478}.
FT DOMAIN 373..447
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 471 AA; 50394 MW; E47E3952D73E2E56 CRC64;
MKDRGVDATS QTANTRPDML TIPDLIRKKR DGGQLSDDEI KAFIQAVKEK TIQDSQIGAM
LMAIWLNGMV SVEIKALTRE MMSSGEVMEW PDEWKNFMVD KHSTGGVGDK VSLVLAPALA
ACGCKVPMIS GRGLAHTGGT LDKLESIPGF KVEQSREQIL EILDSVGCCI VGQTETLVPA
DRVLYALRDI TGTVDSLPLI TSSIISKKGA ESLSALVLDV KFGRAAVCKD LESATELAQM
LVEAGNGLGI RTAAVLSGMN GSIGRCVGNS VEVIESLETL KGNGPDDLME LVTTQGGLLL
VMTGLVSDLS EGRKQISEAV VGGAALSKFQ AMMEAQGVNS DTAQRLCTTN TDYYSVLRKA
KHQLELKAPA DGIVLEIDGL VLAQVLHRLG AGRSKAGEPV NHSVGAVLLV SIGQRVTKGV
SWLRLHYEDP ALTPDQRNHL ESALTVGTDQ KIQTQQKCTL VEKILPKKYA Y
//
