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
//