ID A0A1Y0ICW4_9GAMM Unreviewed; 511 AA.
AC A0A1Y0ICW4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Putative thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00703};
DE EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_00703};
DE AltName: Full=TdRPase {ECO:0000256|HAMAP-Rule:MF_00703};
GN ORFNames=OLMES_4381 {ECO:0000313|EMBL:ARU58378.1};
OS Oleiphilus messinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oleiphilaceae; Oleiphilus.
OX NCBI_TaxID=141451 {ECO:0000313|EMBL:ARU58378.1, ECO:0000313|Proteomes:UP000196027};
RN [1] {ECO:0000313|EMBL:ARU58378.1, ECO:0000313|Proteomes:UP000196027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ME102 {ECO:0000313|EMBL:ARU58378.1,
RC ECO:0000313|Proteomes:UP000196027};
RA Kozyavkin S.A., Slesarev A.I., Golyshin P.N., Korzhenkov A.,
RA Golyshina O.N., Toshchakov S.V.;
RT "Genomic insights into alkan degradation activity of Oleiphilus
RT messinensis.";
RL Submitted (MAY-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, ECO:0000256|HAMAP-
CC Rule:MF_00703};
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. Type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00703}.
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DR EMBL; CP021425; ARU58378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0ICW4; -.
DR KEGG; ome:OLMES_4381; -.
DR OrthoDB; 341217at2; -.
DR Proteomes; UP000196027; Chromosome.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan 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:InterPro.
DR Gene3D; 1.20.970.50; -; 1.
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_00703; Thymid_phosp_2; 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; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR028579; Thym_Pase_Put.
DR InterPro; IPR013466; Thymidine/AMP_Pase.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR NCBIfam; TIGR02645; ARCH_P_rylase; 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 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_00703}; Reference proteome {ECO:0000313|Proteomes:UP000196027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00703}.
FT DOMAIN 437..503
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 511 AA; 54187 MW; 2EC6FCFE1D76B531 CRC64;
MLENYLHLIR PGIDTHQELV VYMRQDCHVC RSEGFTAHSR VRIQVGERSA VATLNIVKGD
FLPHNQAALS EAAWRKLKPE EGEKAYFKHA PAVDSMSAVR GKLYGKPLTT AAAKSVIEDI
NAGHYSDIQL AAFVAACSGN RLTLDETVAI TGAMIDAGQR FKWNSERVLD KHCVGGLPGN
RTTPIVTAII AANGLVMPKT SSRAITSPAG TADTMEVLTD VQLSYDRMAE VVKQTGGCLA
WGGSVSLSPA DDVIIRVERA LDLDSEGQLV ASVISKKVAA GSTHVLIDIP TGPTAKVRSP
EFAARLSELL IGTGAAFGLK VKTIISDGSQ PVGMGIGPAL EARDVLKVLQ CQTDSPQDLR
SRSLAIAAAL LEMSAGNGQR TGTGQSAGNE WLTLATDTLD SGRAYQKFQE ICLAQGRFSE
PELAAHRRTV KATRGGIVSS VNNRILARLA SLAGAPNAKA AGLDLHVRLG DCVTLGDPLL
TVYAEAPGEL EYALDFLMSH PDGVHIGEEA V
//
