ID H2P4X1_PONAB Unreviewed; 487 AA.
AC H2P4X1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 59.
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:ENSPPYP00000013377.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000013377.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000013377.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000013377.2}
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}.
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DR AlphaFoldDB; H2P4X1; -.
DR Ensembl; ENSPPYT00000013923.2; ENSPPYP00000013377.2; ENSPPYG00000011992.2.
DR eggNOG; ENOG502QPRY; Eukaryota.
DR GeneTree; ENSGT00390000009250; -.
DR HOGENOM; CLU_025040_0_2_1; -.
DR InParanoid; H2P4X1; -.
DR OMA; VWGGATN; -.
DR TreeFam; TF332198; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000001595; Chromosome 22.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
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:0046074; P:dTMP catabolic process; IEA:Ensembl.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:Ensembl.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:1905333; P:regulation of gastric motility; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; IEA:Ensembl.
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:UP000001595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000478}.
FT DOMAIN 393..467
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 50465 MW; 0555A2E39F96170D CRC64;
MAASMTPGTG APPAPGDFSG EGSQGLPDPS PEPKQLPELI RMKRDGGRLS EADIRGFVAA
VVNGSAQGAQ IGAMLMAIRL RGMDLEETSV LTQALAQSGQ QLEWPEAWRQ QLVDKHSTGG
VGDKVSLVLA PALAACGCKV PMISGRGLGH TGGTLDKLES IPGFNVIQSP EQMQVLLEQA
GCCIVGQSEQ LVPADGILYA ARDVTATVDS LPLITASILS KKLVEGLSAL VVDVKFGGAA
VFPNQEQARE LAKTLVGVGA SLGLRVAAAL TAMDKPLGRC VGHALEVEEA LLCMDGAGPP
DLRDLVTTLG GALLWLSGHA GTQAQGAARV AAALDDGSAL GRFERMLAAQ GVDPGLARAL
CSGSPAERRQ LLPRAREQEE LLAPADASLP AGTVELVRAL PLALVLHELG AGRSRAGEPL
RLGVGAELLV DVGQRLRRGT PWLRVHRDGP ALSGPQRRAL QKALILSDRA PFAAPSPFAE
LVLPPQQ
//
