ID U1RAY6_9ACTO Unreviewed; 455 AA.
AC U1RAY6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:ERH16808.1};
GN ORFNames=HMPREF0043_01693 {ECO:0000313|EMBL:ERH16808.1};
OS Actinobaculum sp. oral taxon 183 str. F0552.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=1227261 {ECO:0000313|EMBL:ERH16808.1, ECO:0000313|Proteomes:UP000016495};
RN [1] {ECO:0000313|EMBL:ERH16808.1, ECO:0000313|Proteomes:UP000016495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0552 {ECO:0000313|EMBL:ERH16808.1,
RC ECO:0000313|Proteomes:UP000016495};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERH16808.1}.
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DR EMBL; AWSB01000051; ERH16808.1; -; Genomic_DNA.
DR AlphaFoldDB; U1RAY6; -.
DR STRING; 1227261.HMPREF0043_01693; -.
DR PATRIC; fig|1227261.3.peg.1493; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_11; -.
DR Proteomes; UP000016495; 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:UP000016495};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 347..421
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
FT REGION 422..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 47449 MW; DD0446CCBCEC1D68 CRC64;
MRPAGRVDVA EAFDAVDVIR VKRDGGELTD SQIDWVVDAY TRGAVADEQM GALAMAIFLN
GMNRRETARW TDAMIASGER MDFSGLARPT VDKHSTGGVG DKVTLPLAPL VASFGVAVPQ
LSGRGLGHTG GTLDKLESIP GWRAAIPADR IRRQLGEGSG AVVCAAGPGL APADRKLYAL
RDTTCTVDSI PLIASSIMSK KIAEGTEALV LDVKVGSGAF MSTLPQAREL ASTMVELGAD
AGVGTVALLT DMSVPLGLTV GNALEVRESV DVLAGGGPGD VVELTLALAR EMLAAAGLPD
ADPEAALRGG RAMDVWRTMI REQGGDPDAP LPAARETHDV LAENDGILRD LDALKVGVAS
WRLGAGRARK EDPVQAGAGI EIHAKPGDRV RKGDRLLTLH TDDPDRFERA MAALEGTLDI
VVETSRDESA PGREQTPRGA PPPRGSVVLG RVGAP
//
