RBKTP_CUPNH
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 25-MAY-2022, entry version 98.
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; Proteobacteria; 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 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 PRIDE; Q0K3R9; -.
DR EnsemblBacteria; CAJ95355; CAJ95355; 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 OMA; DVWRRMI; -.
DR OrthoDB; 1724909at2; -.
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; 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; 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; 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 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
