ID D3LPH4_MICLU Unreviewed; 444 AA.
AC D3LPH4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:EFD50615.1};
DE EC=2.4.2.4 {ECO:0000313|EMBL:EFD50615.1};
GN Name=deoA {ECO:0000313|EMBL:EFD50615.1};
GN ORFNames=HMPREF0569_0722 {ECO:0000313|EMBL:EFD50615.1};
OS Micrococcus luteus SK58.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=596312 {ECO:0000313|EMBL:EFD50615.1, ECO:0000313|Proteomes:UP000002933};
RN [1] {ECO:0000313|EMBL:EFD50615.1, ECO:0000313|Proteomes:UP000002933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK58 {ECO:0000313|EMBL:EFD50615.1,
RC ECO:0000313|Proteomes:UP000002933};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (NOV-2009) 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:EFD50615.1}.
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DR EMBL; ADCD01000064; EFD50615.1; -; Genomic_DNA.
DR RefSeq; WP_002856560.1; NZ_ADCD01000064.1.
DR AlphaFoldDB; D3LPH4; -.
DR GeneID; 85482264; -.
DR Proteomes; UP000002933; 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; 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 ECO:0000313|EMBL:EFD50615.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFD50615.1}.
FT DOMAIN 349..423
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 444 AA; 46226 MW; B6040AAA12DE7F3E CRC64;
MTAQPQAEPF DAVEVIRTKR DRGTLSPEQI DWVVDAYTRG VVADEQMSAL AMAILLNGMD
RAEIARWTDA MIASGERMDF GGLTTPDGRP LATADKHSTG GVGDKITLPL APLVASFGVA
VPQLSGRGLG HTGGTLDKLE AIPGWRADLS NEAMLRQLSE VGAVICAAGS GLAPADKRLY
ALRDVTGTVE AIPLIASSIM SKKIAEGTGA LVLDVKCGSG AFMKDEASAR ELARTMVDLG
RDAGVDTSAL LTDMSVPLGR TAGNALEVRE SVEVLAGGGP ADVVELTVAL AAAMLAGAGV
TDVDPAEHLA NGRAMDVWNR MIEAQGGDPR AALPTAAHTE DVVAETDGVL TELDAMAVGL
AAWRLGAGRE RQGQAVQAAA GVEVHVRPGE RVAQGQKVLT LHTDTPERFE RARAALAGGW
AVGELDDVDA RTLRERSVIL DRIG
//
