ID I2F2F6_9BACT Unreviewed; 433 AA.
AC I2F2F6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:AFK06109.1};
GN ORFNames=Theba_0381 {ECO:0000313|EMBL:AFK06109.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06109.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK06109.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(2012).
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; CP003532; AFK06109.1; -; Genomic_DNA.
DR RefSeq; WP_014730232.1; NC_017934.1.
DR AlphaFoldDB; I2F2F6; -.
DR STRING; 660470.Theba_0381; -.
DR KEGG; mpg:Theba_0381; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_0; -.
DR Proteomes; UP000002881; 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: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:UP000002881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 345..419
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 433 AA; 46922 MW; 26BD6F20F978534A CRC64;
MRIYDIIMKK RNGFPNTREE LDSLIMGFVE GIVPDYQMAA WLMAVYFNHL NAEERFHLTE
IMIESGDRID LSSIKGRKID KHSTGGVGDK VTLVVGPIVA AAGLVFAKLS GRGLGHTGGT
IDKLESIPGF VTSLDIEQFK RQAERIGIAL AGQTAQVAVA DKKLYALRDL TATVDEISLI
ASSIMSKKLA VDSDGILLDV KIGTGAFMKD LDGAKTLARA MIDLGRKNGR ATKAVISDMN
QPLGVSVGNS LEVVEAIDTL KGRGPQDFSS LCRIIAGQML VAGGMKSEAD ALRTVDRLIL
SGEALRKFDE FVYAQGGPEG FSASYAVHFK EAEIVEEVRT SVSGYVQSVD AESIGLICMR
LGAGRERKED VIDPSVGIRI LKRIGDRVEK DEVIAVIYAN DKRNADNEAK KLVDSFVISE
QKTSPPPIVY EVI
//
