ID H9GH56_ANOCA Unreviewed; 473 AA.
AC H9GH56;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 56.
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:ENSACAP00000010856.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000010856.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000010856.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000010856.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000010856.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 RefSeq; XP_008120562.1; XM_008122355.2.
DR RefSeq; XP_008120563.1; XM_008122356.2.
DR AlphaFoldDB; H9GH56; -.
DR STRING; 28377.ENSACAP00000010856; -.
DR Ensembl; ENSACAT00000011082.4; ENSACAP00000010856.3; ENSACAG00000011062.4.
DR GeneID; 100552690; -.
DR KEGG; acs:100552690; -.
DR CTD; 1890; -.
DR eggNOG; ENOG502QPRY; Eukaryota.
DR GeneTree; ENSGT00390000009250; -.
DR HOGENOM; CLU_025040_0_2_1; -.
DR InParanoid; H9GH56; -.
DR TreeFam; TF332198; -.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000011062; Expressed in kidney and 1 other cell type or tissue.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:UP000001646};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000478}.
FT DOMAIN 371..445
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 473 AA; 50448 MW; 8E2D3709993AB474 CRC64;
MQPYGAMDPN VSSSSRPSML DIIQKKRDGK KLQEEEIGYF VKAVTQGELR DAQIGAMLMA
TWLKGMEPEE TLALTREMAT SGRVLKWPEK WRGLLVDKHS TGGVGDKVSL PLAPALAACG
CKVPMISGRG LGHTGGTLDK LESIPGFRVS QSPEQMKKIL QKVGCCIVEQ SQELVPADKI
LYALRDVTAT VDSVPLATGS ILSKKVAENL SALVLDVKIG NGAVFPTLES AQQLAESLVS
VGTQLGINTV AIFSKMDSPL GRRVGNSLEV LESLECLDGG GPTDLRELVT TLGGTLLWQC
GRAPSVSQGS ARIAKALDDG SALGAFRAML QAQGVDANTA KALCHGTEEQ RLQVLGSPRV
QTALVAHCDG TVHQILAMPI AQVLHALGAG RTKEGQRIQH QVGAELLVSV GERVRKGMPW
IWIHCVSLEL SDANRSTLQS ALIIKDTEPF VPGPKVVKTL LPKVSEVPRK TDT
//