ID A0A0R2XT46_9BACT Unreviewed; 444 AA.
AC A0A0R2XT46;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:KRP37332.1};
GN ORFNames=ABS34_03360 {ECO:0000313|EMBL:KRP37332.1};
OS Opitutaceae bacterium BACL24 MAG-120322-bin51.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=1655636 {ECO:0000313|EMBL:KRP37332.1, ECO:0000313|Proteomes:UP000054041};
RN [1] {ECO:0000313|EMBL:KRP37332.1, ECO:0000313|Proteomes:UP000054041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL24 MAG-120322-bin51 {ECO:0000313|EMBL:KRP37332.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRP37332.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIDO01000022; KRP37332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2XT46; -.
DR Proteomes; UP000054041; 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; 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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 358..429
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 444 AA; 48565 MW; 22E5D1B83E20735D CRC64;
MRKNIISARK FIKPSFSYLV EKKRDGGEFS DEEIRYIVDS ILDDELPEFQ QSALAMAIFF
QGMSAQETAI FAEEMMLSGE VIDLTGISRP KIDKYSTGGV GDKTTLVLGP LAAACGVVMP
TMNGVDEEHV ISNLDKLSSI PNFNPILDLK GFKAQLKTVG CTFIKQDPEI SPVDAKFYKL
RQLTGTIPCL PLITGSVLSR KLAEGAEGLV IDVKWGNGSF IKDVEQAKQL ARSITRVGRS
MKRRCVALVT DMNQPLGDTV GTALEIKEAI QLLKGEGPED LQELVLKLGM EIVRLAGVAG
STLSAKQTVQ RHLRDGSALQ KFKDMVAAQG GDISVIDNPD KFPTAKHVRK LPAPKRGYVH
TINAGLIAEG VQKLAMRKNG TYDPAVGVSE IKKVGTQVKQ GEPLMMIHYN DEAKMEEALE
YLKTAYRLAP KRPNPPVLIV ERVA
//