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Q0K3R9 (RBKTP_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase

Including the following 2 domains:

  1. Ribose 1,5-bisphosphate phosphokinase PhnN
    EC=2.7.4.23
    Alternative name(s):
    Ribose 1,5-bisphosphokinase
  2. Putative thymidine phosphorylase
    EC=2.4.2.4
    Alternative name(s):
    TdRPase
Gene names
Name:phnN
Ordered Locus Names:H16_B0558
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP) By similarity. HAMAP-Rule MF_00703

Catalytic activity

ATP + alpha-D-ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00703

Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_00703

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3. HAMAP-Rule MF_00703

Sequence similarities

In the N-terminal section; belongs to the ribose 1,5-bisphosphokinase family.

In the C-terminal section; belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase HAMAP-Rule MF_00703
PRO_0000314709

Regions

Region1 – 177177Ribose 1,5-bisphosphokinase HAMAP-Rule MF_00703
Region178 – 601424Thymidinephosphorylase HAMAP-Rule MF_00703

Sequences

Sequence LengthMass (Da)Tools
Q0K3R9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 99B7554ACC47C203

FASTA60163,353
        10         20         30         40         50         60 
MKATGTFFFV VGPSGAGKDS LIDGARAALD GDYVFARRVI TRPDGSAGEE HEGVTEAEFA 

        70         80         90        100        110        120 
RRQRSGEFLV TWDAHDLRYG LPKSLMCELE RGRNVVANGS RGVIAELAAR LPRFVVVLVT 

       130        140        150        160        170        180 
APHDVLARRI AARGRESGDQ VASRVARAGA PVPPHVPCIT VSNHSTLEAG TARFVEALRT 

       190        200        210        220        230        240 
GTRTSAAERP ASRTNLMAKL RGEPLDEAAY VAVLQDAIAG RYTEAELTEF LVAATRTLTD 

       250        260        270        280        290        300 
EEVVALARAR TAFTPRIDWD EPVVVDKHSM GGVPGSRITL IVVPIVAAYG LAMPKTSSRA 

       310        320        330        340        350        360 
ITSAAGTADA METIARVDLA HEDVRRCVAQ ARACIAWNGR LNHSVVDDVM NAITRPLRLD 

       370        380        390        400        410        420 
SRRWSVASIL SKKYTAGATH VIVDLPYGPQ TKLATRADAE ALGALFEHVG KGLGLHVRAL 

       430        440        450        460        470        480 
VTDGSGPIGR GIGPALEVRD VRLVLDNAPD APADLRDKAL RFAGEIIAFD PRVDSPEHGM 

       490        500        510        520        530        540 
QIAAALLHEG KARAAFDRIA AAQGVRCDPV APGTHTLVVP ATTRGRVAGV DGLQISGVAR 

       550        560        570        580        590        600 
AAGAPRDGGA GVDMLCAIGA KVAPGQPLYR IHSDSAEALE AAAALVRAGG ECCQAVRIDP 


D 

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References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260480 Genomic DNA. Translation: CAJ95355.1.
RefSeqYP_728720.1. NC_008314.1.

3D structure databases

ProteinModelPortalQ0K3R9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B0558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ95355; CAJ95355; H16_B0558.
GeneID4456323.
KEGGreh:H16_B0558.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMAMNAITRP.
OrthoDBEOG61ZTGG.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-4265-MONOMER.
UniPathwayUPA00087; UER00175.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.40.50.300. 2 hits.
3.90.1170.30. 1 hit.
HAMAPMF_00703. Thymid_phosp_2.
MF_00836. PhnN.
InterProIPR000312. Glycosyl_Trfase_fam3.
IPR027417. P-loop_NTPase.
IPR012699. PhnN.
IPR013102. PYNP_C.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR028579. Thym_Pase_Put.
[Graphical view]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF52418. SSF52418. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR02322. phosphon_PhnN. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBKTP_CUPNH
AccessionPrimary (citable) accession number: Q0K3R9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways