ID A0A255Z466_9PROT Unreviewed; 502 AA.
AC A0A255Z466;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CHU95_05665 {ECO:0000313|EMBL:OYQ36297.1};
OS Niveispirillum lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Niveispirillum.
OX NCBI_TaxID=1981099 {ECO:0000313|EMBL:OYQ36297.1, ECO:0000313|Proteomes:UP000216998};
RN [1] {ECO:0000313|EMBL:OYQ36297.1, ECO:0000313|Proteomes:UP000216998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1-14 {ECO:0000313|Proteomes:UP000216998};
RA Cai H.;
RT "Niveispirillum cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYQ36297.1}.
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DR EMBL; NOXU01000023; OYQ36297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255Z466; -.
DR OrthoDB; 341217at2; -.
DR Proteomes; UP000216998; Unassembled WGS sequence.
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 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_00703}; Reference proteome {ECO:0000313|Proteomes:UP000216998};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00703}.
FT DOMAIN 426..493
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 502 AA; 53188 MW; 5B925168074B5277 CRC64;
MLRLKRIGIS TSRENVAFLS RACTSYRAAA FEGQEKVEVV ANGHRLVATL NLVNDPAILP
PDCLGLSEQA FARFGLAEGT AVRLDHPHPP KSREGLHAKI AGRELDETCF RAIIEDIAHH
RYGKVEVAAF LVACGSFMTT AETLALTRAM ADAGETLHWP GTPLVVDKHC IGGIPGNRTS
MIVVPIVAAH GLPMPKTSSR AITSPAGTAD TMEVLANVEI DLPTMRAIVA EAGGCLVWGG
HVKLSPADDV LISVERPLNI DTREQMVASI LSKKKAAGST HLVIDMPVGP SAKVRTADDA
ARLRKLFEYV GDAIGLSLRV TISDGTQPVG RGIGPVLEAR DVMAVLENRA DAPADLRERS
LALAGRILEF DPALRGGAGL ARARALLDSG AALAKMQQIM ALQGPPPRLA RLGGLSREIV
ADQDGRVLAI DCYRMARIAR LAGAPFDPGA GIDLLKKVGD PVQAGEPLYR IHAEREVEFR
FACGLAAEAS GYAVNGNGKG QN
//
