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Database: UniProt
Entry: A0A369Y546_9FUSO
LinkDB: A0A369Y546_9FUSO
Original site: A0A369Y546_9FUSO 
ID   A0A369Y546_9FUSO        Unreviewed;       433 AA.
AC   A0A369Y546;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:RDE66091.1};
DE            EC=2.4.2.4 {ECO:0000313|EMBL:RDE66091.1};
GN   ORFNames=DV867_01040 {ECO:0000313|EMBL:RDE66091.1};
OS   Psychrilyobacter sp. S5.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Psychrilyobacter.
OX   NCBI_TaxID=2283384 {ECO:0000313|EMBL:RDE66091.1, ECO:0000313|Proteomes:UP000253914};
RN   [1] {ECO:0000313|EMBL:RDE66091.1, ECO:0000313|Proteomes:UP000253914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5 {ECO:0000313|EMBL:RDE66091.1,
RC   ECO:0000313|Proteomes:UP000253914};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Psychrilyobacter sp. strain S5.";
RL   Submitted (JUL-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:RDE66091.1}.
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DR   EMBL; QQOU01000001; RDE66091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369Y546; -.
DR   Proteomes; UP000253914; 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:RDE66091.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253914};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDE66091.1}.
FT   DOMAIN          345..418
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   433 AA;  47205 MW;  FAFAA6004912E0FA CRC64;
     MRIVDIIQKK REKEILTDEE IRFLLENYQA GEVPDYQIAS FLMAVYFNGM TTEELKVFTG
     TMIDSGETID FPGVEKFLID KHSTGGVGDK TTIALAPIFG ALGMGTAKLS GKGLGHTGGT
     IDKFESIKGF KFSNSKEELI KIVNETGTGL MGQADTIVPL DKKLYALRDV TATVSSIPLI
     ASSIMSKKLA VHADAIILDV KVGSGAFMKD LTEARKLAQT MYDLGKAFDR NIVCMLTNMD
     EPLGNAVGNS LEIVEAVETL KGNGPEDFTY LVEVLGAQAL ILKGDVKTLE EGIGRVKEVI
     ENGEALKMLK KFIKGSGGNP DICDDYSLLN IAAETFEFNV DERGYIKHID AEKIGKAAMM
     LGAGRATKDD IIDHSVGLIM HKKVGDQFEA GEALLTLYHQ NNMRDEILET LRGAFVFSEE
     KVEKIPTILD MIG
//
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