ID A0A2U1SWM7_9MICO Unreviewed; 431 AA.
AC A0A2U1SWM7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:PWB95992.1};
GN ORFNames=DF220_11355 {ECO:0000313|EMBL:PWB95992.1};
OS Salinibacterium hongtaonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Salinibacterium.
OX NCBI_TaxID=2079791 {ECO:0000313|EMBL:PWB95992.1, ECO:0000313|Proteomes:UP000244978};
RN [1] {ECO:0000313|Proteomes:UP000244978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1194 {ECO:0000313|Proteomes:UP000244978};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-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:PWB95992.1}.
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DR EMBL; QEEX01000002; PWB95992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1SWM7; -.
DR Proteomes; UP000244978; 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; IPR017872; Pyrmidine_PPase_CS.
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.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000244978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 339..413
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 431 AA; 45239 MW; F3379C1120CCEBF3 CRC64;
MAIEPFDTVD LIRTKRDKGA LSTEQIDWLI DAYTRGYVGD EQMAAMTMAI FLNGMKREEI
RDLTLAMIAS GERMNFDSLS KVTTDKHSTG GVGDKITLPL APLVASFGVA VPQLSGRGLG
HTGGTLDKLE AIPGWRADLS NDEFFAQLEE VGSVICAAGA GLAPADKKLY ALRDITSTVE
AIPLIASSIM SKKIAEGTAS LVLDVKFGSG AFLKDPARSR ELAQTMVALG KDAGVATVAL
LTNMNVPLGL AIGNANEVRE SVEVLAGGGP ADVVELTIAL AREMLALAGQ PDADVEAALK
DGRAMDTWNA MIRAQGGDPD AALPVAKETH VVTAPRSGVL VQQEALPFGV AAWRLGAGRA
RKQDPVQHAA GIDLHAKPGD TVVEGQPLFT LSADEPERFA RALEALEGSW RIGDEGDAID
DGGPLIADRI A
//
