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Database: UniProt
Entry: U1GLW0_9ACTN
LinkDB: U1GLW0_9ACTN
Original site: U1GLW0_9ACTN 
ID   U1GLW0_9ACTN            Unreviewed;       325 AA.
AC   U1GLW0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:ERF57759.1};
DE            EC=2.4.2.4 {ECO:0000313|EMBL:ERF57759.1};
DE   Flags: Fragment;
GN   Name=deoA {ECO:0000313|EMBL:ERF57759.1};
GN   ORFNames=H641_02433 {ECO:0000313|EMBL:ERF57759.1};
OS   Cutibacterium granulosum DSM 20700.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF57759.1, ECO:0000313|Proteomes:UP000016307};
RN   [1] {ECO:0000313|EMBL:ERF57759.1, ECO:0000313|Proteomes:UP000016307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF57759.1,
RC   ECO:0000313|Proteomes:UP000016307};
RX   PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA   Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA   Brinkmann V., Meyer T.F., Bruggemann H.;
RT   "Comparative genomics reveals distinct host-interacting traits of three
RT   major human-associated propionibacteria.";
RL   BMC Genomics 14:640-640(2013).
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:ERF57759.1}.
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DR   EMBL; AOSS01000066; ERF57759.1; -; Genomic_DNA.
DR   RefSeq; WP_021103505.1; NZ_AOSS01000066.1.
DR   AlphaFoldDB; U1GLW0; -.
DR   PATRIC; fig|1160719.4.peg.465; -.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000016307; 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-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; IPR035902; Nuc_phospho_transferase.
DR   InterPro; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:ERF57759.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016307};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERF57759.1}.
FT   DOMAIN          237..311
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ERF57759.1"
SQ   SEQUENCE   325 AA;  33366 MW;  75B1AF12D261E17F CRC64;
     PLVAACGAAV PQLSGRGLGH TGGTLDKMEA IPGWRANLTH DEMMRQLEEV GAVVCAAGPG
     LAPADKKLYA LRDVTGTVES IPLIASSIMS KKIAEGTDAL VLDVKTGSGA FMKTEEDSRE
     LARRLVGLGK AAGVNTSALI TRMDVPLGYA CGNGIEVAEA IEVLAGGGPS DVVELTVALA
     RRMVEAAGLD ADPEQVLASG AAMDVWRAMI RAQGGDPDAA LPIAKHSDDL HAPHDGVVTD
     IDAMSVGIAA WRLGAGRARK EDPVQAAAGV LLRVRPGDRV VTGQPLATLL TDTPEAVDRA
     QAALEGAFTL GDSSDCRPIV VGHVD
//
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