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Q46UT0 (RBKTP_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Reut_B3746
OrganismCupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus ›

Protein attributes

Sequence length602 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 caution

The sequence AAZ63104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602Bifunctional ribose 1,5-bisphosphokinase-thymidine phosphorylase HAMAP-Rule MF_00703
PRO_0000314710

Regions

Region1 – 187187Ribose 1,5-bisphosphokinase HAMAP-Rule MF_00703
Region188 – 602415Thymidinephosphorylase HAMAP-Rule MF_00703

Sequences

Sequence LengthMass (Da)Tools
Q46UT0 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: D622AFD8F873E7CA

FASTA60263,580
        10         20         30         40         50         60 
MKESGTFFLV VGPSGAGKDS LIDGARATLG NDEYVFARRI ITRPSGSPGE DHESVAEAEF 

        70         80         90        100        110        120 
AERERNGEFL VTWHAHGLRY GLPQWLVGLL ETGKHVVANG SRGVIAMLAR QLPRFVVVNV 

       130        140        150        160        170        180 
TAPQDVLAQR IAARGRESGD DVMRRVARQA PPMPDGVHCV TVTNDSTLDL GVARFTDALR 

       190        200        210        220        230        240 
NGANAGSVPQ PASRRHLAAK LDGQPLDEGA YEAILRDAIA GRYTAQELTA FLTAATRSLD 

       250        260        270        280        290        300 
DREVVALARA RTRFTARIEW DEPIVVDKHS MGGIPGSRIT LIVVPIVAAY GLAMPKTSSR 

       310        320        330        340        350        360 
AITSAAGTAD AMETVARVDL THDDVRRCVA QARACIAWNG RLNHSVIDDV MNAITRPLGL 

       370        380        390        400        410        420 
DSRRWAVASI LSKKATAGAT HVIVDIPYGP QTKLSARADA DALAGLFEEV GKGLGLHVRA 

       430        440        450        460        470        480 
LVTDGSRPIG RGVGPALEVR DVRQVLENHP DAPMDLREKA LRFAGEIIAF DPRVASAAQG 

       490        500        510        520        530        540 
MRIATALLDE GSARAAFDRI VATQGIRPDP VAPGAHTHVI VAPAEGRVAA INGWQISGIA 

       550        560        570        580        590        600 
RAAGAPRSAG AGIDLLCTIG ERVAAGEPLY RIHAESAADL ATAVAMTGPA GEASTAVRVD 


PD

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References

[1]"Complete sequence of chromosome 2 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000091 Genomic DNA. Translation: AAZ63104.1. Different initiation.
RefSeqYP_297948.1. NC_007348.1.

3D structure databases

ProteinModelPortalQ46UT0.
ModBaseSearch...

Protein-protein interaction databases

STRING264198.Reut_B3746.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ63104; AAZ63104; Reut_B3746.
GeneID3613838.
KEGGreu:Reut_B3746.
PATRIC20233289. VBIRalEut24049_4448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-3820-MONOMER.
UniPathwayUPA00087; UER00175.

Family and domain databases

Gene3D3.40.1030.10. 2 hits.
3.90.1170.30. 1 hit.
HAMAPMF_00703. Thymid_phosp_2. Fused.
MF_00836. PhnN. Fused.
InterProIPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR027417. P-loop_NTPase.
IPR012699. PhnN.
IPR013102. PYNP_C.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR013466. Thymidine_Pase_type2.
[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]
SUPFAMSSF47648. Glyco_trans_3. 1 hit.
SSF52418. Glyco_trans_3. 1 hit.
SSF54680. PYNP_C. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR02322. phosphon_PhnN. 1 hit.
PROSITEPS50052. GUANYLATE_KINASE_2. False negative.
PS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBKTP_CUPPJ
AccessionPrimary (citable) accession number: Q46UT0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: May 29, 2013
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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