ID A0A402B3N3_9CHLR Unreviewed; 435 AA.
AC A0A402B3N3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:GCE25952.1};
GN ORFNames=KDA_14360 {ECO:0000313|EMBL:GCE25952.1};
OS Dictyobacter alpinus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=2014873 {ECO:0000313|EMBL:GCE25952.1, ECO:0000313|Proteomes:UP000287171};
RN [1] {ECO:0000313|Proteomes:UP000287171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno16 {ECO:0000313|Proteomes:UP000287171};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:GCE25952.1}.
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DR EMBL; BIFT01000001; GCE25952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402B3N3; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000287171; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000287171};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 435 AA; 46020 MW; A36F8D7B1A869AD8 CRC64;
MQTVELITKK RDGGTFSTDE IRWLIAQYTQ GTIPDYQMAS LLMAIYLRGM DARETSDLTL
AMVNSGEQLR VNTLVSPVVD KHSTGGVGDK VTLAVAPLVA ACGVAVGKMT GRGLGHTGGT
VDKLESVTGF HVELSRADFM RILQEHQIVL AGQSSDLAPA DGKLYALRDV TGTIESIPLI
ASSIMSKKLA IGASHLLLDV KFGSGAFMKT IEQARELAQA MVEIGRAGNL HTVAAITSME
QPLGYAVGNA IELREAIDIL HGQGPADVSE LCYHEAAELL VMTGKAADLA EADQLVANAI
QSGAAVKKLA EVIAAQGGDA RQIENPDLLP SAPIRVMLPA TQTGYIAAIN AEGIGLASMS
LGAGRFKKGE PVDHRTGLLL KAKIGDHVNA GDPLIEIHAR NPEEAQQIQS ALLACYQWSE
TPVQVQPLIC DVIRP
//