RBKTP_CUPTR
ID RBKTP_CUPTR Reviewed; 601 AA.
AC B2AIF3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase;
DE Includes:
DE RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN;
DE EC=2.7.4.23;
DE AltName: Full=Ribose 1,5-bisphosphokinase;
DE Includes:
DE RecName: Full=Putative thymidine phosphorylase;
DE EC=2.4.2.4;
DE AltName: Full=TdRPase;
GN Name=phnN; OrderedLocusNames=RALTA_B0356;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-
CC ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:68688, ChEBI:CHEBI:456216;
CC EC=2.7.4.23;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.4;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route II): step 3/3.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribose 1,5-
CC bisphosphokinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU633750; CAP63552.1; -; Genomic_DNA.
DR RefSeq; WP_012355206.1; NC_010530.1.
DR AlphaFoldDB; B2AIF3; -.
DR SMR; B2AIF3; -.
DR STRING; 977880.RALTA_B0356; -.
DR EnsemblBacteria; CAP63552; CAP63552; RALTA_B0356.
DR GeneID; 29765621; -.
DR KEGG; cti:RALTA_B0356; -.
DR eggNOG; COG0213; Bacteria.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_025040_6_0_4; -.
DR OMA; HDDVRRC; -.
DR OrthoDB; 1724909at2; -.
DR BioCyc; CTAI977880:RALTA_RS17480-MON; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000001692; Chromosome 2.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019634; P:organic phosphonate metabolic process; IEA:UniProtKB-UniRule.
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; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.90.1170.30; -; 1.
DR HAMAP; MF_00836; PhnN; 1.
DR HAMAP; MF_00703; Thymid_phosp_2; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012699; PhnN.
DR InterPro; IPR036566; PYNP-like_C_sf.
DR InterPro; IPR013102; PYNP_C.
DR InterPro; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR028579; Thym_Pase_Put.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR PANTHER; PTHR10515; PTHR10515; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF07831; PYNP_C; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02322; phosphon_PhnN; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycosyltransferase; Nucleotide-binding; Transferase.
FT CHAIN 1..601
FT /note="Bifunctional ribose 1,5-bisphosphokinase-thymidine
FT phosphorylase"
FT /id="PRO_0000412779"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 601 AA; 63485 MW; 2C4BD4BA05B4E774 CRC64;
MNASGTFFFV VGPSGAGKDA LMDGARAALD DNYVFARRVI TRPEGAVGEA HEAVSEAEFA
RRQRSGEFLV TWDAHDLRYG LPCSLMSELE RGRHVVANGS RAVIAELAQR LPRFVVVLVT
APQDVLARRI AARGRESGEQ IARRVARTGA ALPPEVRCLT VLNDSTLEVG RARFVEALRH
GTRVASDGAP ASRTNLMAKL RGEPLDQAAY VAVLQDAMAG RYTEAELTEF LVAATRSLDD
QEVVALARAR TVFTPRIKWD EPIVVDKHSI GGVPGSRITL IVVPIVAAYG LAMPKTSSRA
ITSAAGTADA METVARVDLA HDDVRRCVAQ ARACIAWNGR LNHSVVDDVM NAITRPLRLD
SRRWAVASIL SKKYTAGATH VIVDLPYGPQ TKLATRADAE ALGAMFEHVG KGLGLHVRAL
VTDGSRPIGR GIGPALEVRD VRQVLANDPC APADLREKAL RFAGEIIAFD ARVGSPAEGL
RIATALLSEG KAKAAFDRIA ATQGARPEPV APGAHTCVVS ATMQGRVAAI DGLRISGVAR
AAGAPRELGA GVDLLCTIGA KVESGQPLYR IHAGSDAALA AAAALARAGG ECSEAVRIDP
D
