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Database: UniProt
Entry: G8NW12_GRAMM
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Original site: G8NW12_GRAMM 
ID   G8NW12_GRAMM            Unreviewed;       474 AA.
AC   G8NW12;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:AEU35432.1};
DE            EC=2.4.2.4 {ECO:0000313|EMBL:AEU35432.1};
GN   OrderedLocusNames=AciX8_1086 {ECO:0000313|EMBL:AEU35432.1};
OS   Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU35432.1, ECO:0000313|Proteomes:UP000007113};
RN   [1] {ECO:0000313|EMBL:AEU35432.1, ECO:0000313|Proteomes:UP000007113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC   {ECO:0000313|Proteomes:UP000007113};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA   Haggblom M., Woyke T.;
RT   "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; CP003130; AEU35432.1; -; Genomic_DNA.
DR   RefSeq; WP_014264312.1; NC_016631.1.
DR   AlphaFoldDB; G8NW12; -.
DR   STRING; 682795.AciX8_1086; -.
DR   KEGG; gma:AciX8_1086; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_0; -.
DR   OrthoDB; 9763887at2; -.
DR   Proteomes; UP000007113; Chromosome.
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; 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; 2.
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   ECO:0000313|EMBL:AEU35432.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEU35432.1}.
FT   DOMAIN          379..453
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   474 AA;  51161 MW;  A5B55639ADFC5FA1 CRC64;
     MSDHAIYPLD IVIKKRDGAE LTKAEIEHFI HAVVLNGEQK LAEARGEKPA TLSATDKVTD
     AQIAAFLMAV FQRGLSPEEL ANLTTAMRFS GETFDAAPLH TFTVDKHSTG GVGDKSSLLI
     APIVAAAGLD LSPSISVPMI SGRSLGHTGG TLDKLETIPG FDTQISMARF AEILRECHAS
     LVGQTPRLVP ADRILYAMRD HTGTVESPFL ITASIMSKKL AESLNALVLD VKVGSGAFMP
     TYEKSKFLAE LMVSTGERAG TRTAALLTTM DEPLGRFSGN WMEVWECVDI LQNRRHPMSA
     DLIELSNILS GWMLYFGGKT ATPEAGAKLA DDILRSGAAY KSWLQIVAAH QGDTSIFNDP
     AAFHQPKATR VLKASRAGYL AGMDCKEVGW AVQRLGAGRA KPGDPVSAHA GIESHAKLGD
     KVEEGQPIFT LFSEDAALLD EPYRMLEATV EIANEPRQKQ PLIREIITKE NIKG
//
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