ID C1B161_RHOOB Unreviewed; 431 AA.
AC C1B161;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Pyrimidine nucleoside phosphorylase {ECO:0000313|EMBL:BAH54556.1};
DE EC=2.4.2.2 {ECO:0000313|EMBL:BAH54556.1};
GN Name=pdp {ECO:0000313|EMBL:BAH54556.1};
GN OrderedLocusNames=ROP_63090 {ECO:0000313|EMBL:BAH54556.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH54556.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH54556.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH54556.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH54556.1; -; Genomic_DNA.
DR RefSeq; WP_015890012.1; NC_012522.1.
DR AlphaFoldDB; C1B161; -.
DR STRING; 632772.ROP_63090; -.
DR KEGG; rop:ROP_63090; -.
DR PATRIC; fig|632772.20.peg.6587; -.
DR HOGENOM; CLU_025040_0_1_11; -.
DR OrthoDB; 9763887at2; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0016154; F:pyrimidine-nucleoside 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; 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 ECO:0000313|EMBL:BAH54556.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAH54556.1}.
FT DOMAIN 337..411
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 431 AA; 44798 MW; 76F6D7AD997EB425 CRC64;
MHDASSIIAA KRDGRELSGA EIDWVVEAFT RGVVADEQMS ALAMAIFFRG MTRGEVSRWT
TAMISSGHRL DFTHLGRPTV DKHSTGGVGD KITLPLAPLV AACGAAVPQL SGRGLGHTGG
TLDKLESIPG WRADLDTSEM AEILSDPEVG AVVCAAGSDL APADRRLYAL RDVTGTVESI
PLIASSIMSK KIAEGTGALV LDVKVGSGAF MKKLDDAREL AQTMVDLGSD AGVRTMAVLT
AMDAPLGHTA GNALEVRESL EVLAGGGPSD VVELTLALAR EMLKAAGIDG VDPADKLRDG
SAMDRWRRMI AAQGGDPYAP LPTARHTEVL LSESDGVVCG LDAMAVGLAA WRLGAGRARQ
GEPVQAGAGI ELHAKPGETV SVGTPLVTLH TDTPERFAAA KAALSEAWTV VADAPPVTTP
LVIERIEDPS R
//
