GenomeNet

Database: UniProt
Entry: A0A0Q9YNQ4_9COXI
LinkDB: A0A0Q9YNQ4_9COXI
Original site: A0A0Q9YNQ4_9COXI 
ID   A0A0Q9YNQ4_9COXI        Unreviewed;       502 AA.
AC   A0A0Q9YNQ4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   Name=pdp {ECO:0000313|EMBL:KRG21545.1};
GN   ORFNames=HT99x_01298 {ECO:0000313|EMBL:KRG21545.1};
OS   Candidatus Berkiella aquae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Berkiella.
OX   NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG21545.1, ECO:0000313|Proteomes:UP000051497};
RN   [1] {ECO:0000313|EMBL:KRG21545.1, ECO:0000313|Proteomes:UP000051497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HT99 {ECO:0000313|EMBL:KRG21545.1,
RC   ECO:0000313|Proteomes:UP000051497};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-2015) 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:KRG21545.1}.
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   EMBL; LKAJ01000004; KRG21545.1; -; Genomic_DNA.
DR   RefSeq; WP_075065927.1; NZ_LKAJ02000001.1.
DR   AlphaFoldDB; A0A0Q9YNQ4; -.
DR   STRING; 295108.HT99x_01298; -.
DR   PATRIC; fig|1590043.3.peg.1316; -.
DR   OrthoDB; 341217at2; -.
DR   Proteomes; UP000051497; 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:UP000051497};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00703}.
FT   DOMAIN          429..496
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   502 AA;  54464 MW;  3899F842952AAAB2 CRC64;
     MTKANTLTLK PLGINTYKEA VVYMRKDCPV CRSEGFEAPA RVKVIHKNKI ILATLNTIES
     DLLTPHEASL STFAWEQLSA SIGDEIQVFH PDHLNSLDHI RGKIYGHELN KDEIREIIKD
     VVNGSLSDIH ISAFLASTGD DRFSEQEIFY LTESMIEVGN RISWHKDLIV DKHCIGGLPG
     NRTTLIVVPI VAAFGLTIPK TSSRAITSPA GTADTMEVFA PVSLDLNAMR KVIEKENGCL
     VWGGSVNLSP ADDILIRIER ALILDSMGQL VASILSKKIA AGSSHVIIDV PIGPTVKVRT
     TASADELKNY LEAIGKTLGI EVKTVFTDGS QPVGRGIGPA LEAKDVLAVL QGDINAPQSL
     RERSIALAGQ VLEFSPNVRK GTGYAVAEKI LSSGQAWQKF QAICHAQGGL FEPPIAKHMR
     TITSKKKGTI LAIDNRYLSR VAKLAGAPQA KAAGIKLLTP IGTKVNFGDP LFEIHAETKG
     ELHYAVNFLS MDHEIFDIGE FE
//
DBGET integrated database retrieval system