ID   RBKTP_CUPNH             Reviewed;         601 AA.
AC   Q0K3R9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=H16_B0558;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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; AM260480; CAJ95355.1; -; Genomic_DNA.
DR   RefSeq; WP_011616677.1; NZ_CP039288.1.
DR   AlphaFoldDB; Q0K3R9; -.
DR   SMR; Q0K3R9; -.
DR   STRING; 381666.H16_B0558; -.
DR   GeneID; 57646446; -.
DR   KEGG; reh:H16_B0558; -.
DR   eggNOG; COG0213; Bacteria.
DR   eggNOG; COG3709; Bacteria.
DR   HOGENOM; CLU_025040_6_0_4; -.
DR   OrthoDB; 341217at2; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000008210; 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:0015716; P:organic phosphonate transport; IEA:UniProtKB-KW.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.970.50; -; 1.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR   HAMAP; MF_00836; PhnN; 1.
DR   HAMAP; MF_00703; Thymid_phosp_2; 1.
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   NCBIfam; TIGR02322; phosphon_PhnN; 1.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Alkylphosphonate uptake; ATP-binding; Glycosyltransferase;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..601
FT                   /note="Bifunctional ribose 1,5-bisphosphokinase-thymidine
FT                   phosphorylase"
FT                   /id="PRO_0000314709"
FT   REGION          1..177
FT                   /note="Ribose 1,5-bisphosphokinase"
FT   REGION          178..601
FT                   /note="Thymidinephosphorylase"
SQ   SEQUENCE   601 AA;  63353 MW;  99B7554ACC47C203 CRC64;
     MKATGTFFFV VGPSGAGKDS LIDGARAALD GDYVFARRVI TRPDGSAGEE HEGVTEAEFA
     RRQRSGEFLV TWDAHDLRYG LPKSLMCELE RGRNVVANGS RGVIAELAAR LPRFVVVLVT
     APHDVLARRI AARGRESGDQ VASRVARAGA PVPPHVPCIT VSNHSTLEAG TARFVEALRT
     GTRTSAAERP ASRTNLMAKL RGEPLDEAAY VAVLQDAIAG RYTEAELTEF LVAATRTLTD
     EEVVALARAR TAFTPRIDWD EPVVVDKHSM GGVPGSRITL IVVPIVAAYG LAMPKTSSRA
     ITSAAGTADA METIARVDLA HEDVRRCVAQ ARACIAWNGR LNHSVVDDVM NAITRPLRLD
     SRRWSVASIL SKKYTAGATH VIVDLPYGPQ TKLATRADAE ALGALFEHVG KGLGLHVRAL
     VTDGSGPIGR GIGPALEVRD VRLVLDNAPD APADLRDKAL RFAGEIIAFD PRVDSPEHGM
     QIAAALLHEG KARAAFDRIA AAQGVRCDPV APGTHTLVVP ATTRGRVAGV DGLQISGVAR
     AAGAPRDGGA GVDMLCAIGA KVAPGQPLYR IHSDSAEALE AAAALVRAGG ECCQAVRIDP
     D
//