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Protein

Phosphoribulokinase 1

Gene

prkA

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate.

Enzyme regulationi

Activated by NADH and inhibited by phosphoenolpyruvate.

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 209ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Calvin cycle, Photosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribulokinase 1 (EC:2.7.1.19)
Short name:
PRK I
Short name:
PRKase 1
Alternative name(s):
Phosphopentokinase 1
Gene namesi
Name:prkA
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Phosphoribulokinase 1PRO_0000201957Add
BLAST

Interactioni

Subunit structurei

Homooctamer.

Protein-protein interaction databases

STRINGi349102.Rsph17025_2714.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126Combined sources
Helixi21 – 3212Combined sources
Beta strandi36 – 405Combined sources
Helixi41 – 444Combined sources
Helixi49 – 6214Combined sources
Helixi72 – 743Combined sources
Helixi77 – 9014Combined sources
Beta strandi126 – 1338Combined sources
Helixi145 – 1473Combined sources
Beta strandi149 – 1568Combined sources
Helixi158 – 16811Combined sources
Beta strandi170 – 1723Combined sources
Helixi180 – 19415Combined sources
Helixi196 – 2005Combined sources
Beta strandi203 – 21210Combined sources
Helixi217 – 2193Combined sources
Helixi226 – 2283Combined sources
Beta strandi229 – 2379Combined sources
Helixi243 – 2497Combined sources
Beta strandi254 – 2574Combined sources
Beta strandi260 – 2645Combined sources
Helixi265 – 2673Combined sources
Helixi268 – 28417Combined sources
Turni285 – 2884Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7JX-ray2.50A1-290[»]
ProteinModelPortaliP12033.
SMRiP12033. Positions 2-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12033.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphoribulokinase family.Curated

Phylogenomic databases

eggNOGiENOG4105CJE. Bacteria.
COG3954. LUCA.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR006082. PRK.
IPR006083. PRK/URK.
[Graphical view]
PfamiPF00485. PRK. 1 hit.
[Graphical view]
PRINTSiPR00478. PHRIBLKINASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00567. PHOSPHORIBULOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKHPIISV TGSSGAGTST VKHTFDQIFR REGVKAVSIE GDAFHRFNRA
60 70 80 90 100
DMKAELDRRY AAGDATFSHF SYEANELKEL ERVFREYGET GQGRTRTYVH
110 120 130 140 150
DDAEAARTGV APGNFTDWRD FDSDSHLLFY EGLHGAVVNS EVNIAGLADL
160 170 180 190 200
KIGVVPVINL EWIQKIHRDR ATRGYTTEAV TDVILRRMHA YVHCIVPQFS
210 220 230 240 250
QTDINFQRVP VVDTSNPFIA RWIPTADESV VVIRFRNPRG IDFPYLTSMI
260 270 280 290
HGSWMSRANS IVVPGNKLDL AMQLILTPLI DRVVRESKVA
Length:290
Mass (Da):32,664
Last modified:August 1, 1992 - v2
Checksum:i6899EFB1D780640F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64624 Genomic DNA. Translation: AAA26113.1.
M28006 Genomic DNA. Translation: AAA26153.1.
PIRiC40767. KIRFAS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64624 Genomic DNA. Translation: AAA26113.1.
M28006 Genomic DNA. Translation: AAA26153.1.
PIRiC40767. KIRFAS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7JX-ray2.50A1-290[»]
ProteinModelPortaliP12033.
SMRiP12033. Positions 2-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349102.Rsph17025_2714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CJE. Bacteria.
COG3954. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00116.

Miscellaneous databases

EvolutionaryTraceiP12033.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR006082. PRK.
IPR006083. PRK/URK.
[Graphical view]
PfamiPF00485. PRK. 1 hit.
[Graphical view]
PRINTSiPR00478. PHRIBLKINASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00567. PHOSPHORIBULOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides."
    Gibson J.L., Falcone D.L., Tabita F.R.
    J. Biol. Chem. 266:14646-14653(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of the gene for phosphoribulokinase activity from Rhodobacter sphaeroides and its expression in Escherichia coli."
    Hallenbeck P.L., Kaplan S.
    J. Bacteriol. 169:3669-3678(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  3. "The crystal structure of phosphoribulokinase from Rhodobacter sphaeroides reveals a fold similar to that of adenylate kinase."
    Harrison D.H., Runquist J.A., Holub A., Miziorko H.M.
    Biochemistry 37:5074-5085(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiKPPR1_RHOSH
AccessioniPrimary (citable) accession number: P12033
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1992
Last modified: December 9, 2015
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Is not found in cells cultured chemoheterotrophically and only low levels of activities are found in those grown photoheterotrophically on oxidized organic acids.

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.