ID A0A1S2MPB3_9MICO Unreviewed; 430 AA.
AC A0A1S2MPB3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:OIJ31917.1};
GN ORFNames=BK819_13885 {ECO:0000313|EMBL:OIJ31917.1};
OS Microbacterium sp. LCT-H2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1914306 {ECO:0000313|EMBL:OIJ31917.1, ECO:0000313|Proteomes:UP000179624};
RN [1] {ECO:0000313|EMBL:OIJ31917.1, ECO:0000313|Proteomes:UP000179624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCT-H2 {ECO:0000313|EMBL:OIJ31917.1,
RC ECO:0000313|Proteomes:UP000179624};
RA Huang B.;
RT "Draft genome sequence of strain LCT isolated from the Shenzhou X
RT spacecraft of China.";
RL Submitted (OCT-2016) 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:OIJ31917.1}.
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DR EMBL; MODW01000006; OIJ31917.1; -; Genomic_DNA.
DR RefSeq; WP_071329661.1; NZ_MODW01000006.1.
DR AlphaFoldDB; A0A1S2MPB3; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000179624; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 340..414
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 430 AA; 45098 MW; 5067FF70FC1C54A6 CRC64;
MTVEPFDAVD VIRAKRDGGV VPEPALRWMV DAYTRGYVSD AQMASFAMAI FQRGMERDEI
RVLTDAMIAS GERMSFATLG KKTVDKHSTG GVGDKITLPL APLVASFGVA VPQLSGRGLG
HTGGTLDKLE SIPGWRAALS NEEMFAQMQG DVGAVICAAG SGLAPADKKL YALRDVTGTV
EAIPLIASSI MSKKIAEGTD ALVLDVKFGS GAFMQDIDRA RELARTMVAL GTDSGVATTA
LLTDMNVPLG RAIGNANEVR ESVEILAGGG PADVRELTVG LAREMLALAG QPDADVEAAL
DDGRAMDTWK AMIRAQDGDP DAALPVARET HVVTAPADGI VTRMDALPFG IAAWRLGAGR
ARAEDPVIFE AGIDLHAKPG DRVSAGQPLF TLSAADEARF PRAIEALEGA WELGDDAPTL
GPIVRERITA
//