ID A0A0D0HZW3_9MICO Unreviewed; 434 AA.
AC A0A0D0HZW3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:KIP53116.1};
GN ORFNames=SD72_04560 {ECO:0000313|EMBL:KIP53116.1};
OS Leucobacter komagatae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=55969 {ECO:0000313|EMBL:KIP53116.1, ECO:0000313|Proteomes:UP000032120};
RN [1] {ECO:0000313|EMBL:KIP53116.1, ECO:0000313|Proteomes:UP000032120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM ST2845 {ECO:0000313|EMBL:KIP53116.1,
RC ECO:0000313|Proteomes:UP000032120};
RA Karlyshev A.V., Kudryashova E.B.;
RT "Draft genome sequence of Leucobacter komagatae strain VKM ST2845.";
RL Submitted (JAN-2015) 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:KIP53116.1}.
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DR EMBL; JXSQ01000004; KIP53116.1; -; Genomic_DNA.
DR RefSeq; WP_042543256.1; NZ_JXSQ01000004.1.
DR AlphaFoldDB; A0A0D0HZW3; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000032120; 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:UP000032120};
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 434 AA; 45033 MW; 20936B6C1D64DE76 CRC64;
MSVEPFDAVD VIRAKRDGGA VPEPALRWMI DAYTRGYVSD AQMASFAMAI FQRGMVRDEI
RVLTDAMINS GERMSFAGLS KPTVDKHSTG GVGDKITLPL APLVAAFGVA VPQLSGRGLG
HTGGTLDKLE AIPGWRAALS NEEMFAQLDG EAGAVICAAG SGLAPADKKL YALRDVTGTV
DSIPLIASSI MSKKIAEGTD ALVLDVKFGS GAFMQDYAMA RELAETMVAL GTDSGVRTSA
LLTDMNVPLG FTIGNANEVR ESVEVLAGGG PADVRELTLA LAREMLALAG QPDADVAAAL
DDGRAMDSWR AMIAAQGGDP DGQLPVARET HVVTAPTSGV MSKLEGLPFG IAAWRLGAGR
ARAEDPVIHS AGIDLHAKPG DTVTAGQPLF TLSAEDAARF PRALETLDGA WEIDADAAPG
AHAPGPLVRE HITG
//
