ID A0A3A9ZEK1_9ACTN Unreviewed; 438 AA.
AC A0A3A9ZEK1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:RKN46892.1};
DE EC=2.4.2.4 {ECO:0000313|EMBL:RKN46892.1};
GN ORFNames=D7294_01380 {ECO:0000313|EMBL:RKN46892.1};
OS Streptomyces hoynatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1141874 {ECO:0000313|EMBL:RKN46892.1, ECO:0000313|Proteomes:UP000272474};
RN [1] {ECO:0000313|EMBL:RKN46892.1, ECO:0000313|Proteomes:UP000272474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 29097 {ECO:0000313|EMBL:RKN46892.1,
RC ECO:0000313|Proteomes:UP000272474};
RX PubMed=24243968; DOI=10.1099/ijs.0.055640-0;
RA Veyisoglu A., Sahin N.;
RT "Streptomyces hoynatensis sp. nov., isolated from deep marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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:RKN46892.1}.
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DR EMBL; RBAL01000001; RKN46892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9ZEK1; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000272474; Unassembled WGS sequence.
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-EC.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:RKN46892.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272474};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RKN46892.1}.
FT DOMAIN 340..414
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 438 AA; 44857 MW; 8D9C8C391AEDF4A4 CRC64;
MSHAGSFDAI TVIRAKRDGH ALAKDQIDWV LDAYVRGEVA EEQMAALAMA ILLNGMDRRE
IADWTAAMIA SGERMDFSSL PLPTTDKHST GGVGDKITLP LAPLVAACGA AVPQLSGRGL
GHSGGTLDKL ESIPGWRARL SAGEMLGVLR EAGAVICAAG EGLAPADRKL YALRDVTGTV
ESIPLIASSI MSKKIAEGTG ALVLDVKVGS GAFMKTYEDA RELAGTMVGL GTDHGVRTVA
LLTEMSVPLG LTAGNALEVR ESVEVLAGGG PADVVELTLA LAREMLDAAG LPDADPAAAL
ADGSAMDRWR RMIRAQGGDP DAPLPTARER HTVPAPASGV LTALDAYAVG VAAWRLGAGR
ARKEDPVQAA AGVELHAKPG DRVAAGAPLL TLHTDTPERF EAALAALGTE GAIAVAPEGS
AEAAAWAGPR PTVLGRIA
//
