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Q9PJ29 (PROB_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Glutamate 5-kinase

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase
Short name=GK
Gene names
Name:proB
Ordered Locus Names:Cj0097
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline By similarity. HAMAP-Rule MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00456.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109656

Regions

Nucleotide binding162 – 1632ATP HAMAP-Rule MF_00456
Nucleotide binding168 – 1736ATP HAMAP-Rule MF_00456
Nucleotide binding204 – 2107ATP HAMAP-Rule MF_00456

Sites

Binding site71ATP By similarity
Binding site451Substrate By similarity
Binding site1301Substrate By similarity
Binding site1421Substrate; via amide nitrogen By similarity

Secondary structure

................................................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9PJ29 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D07802E92023A241

FASTA25127,843
        10         20         30         40         50         60 
MKRIVVKVGS HVISEENTLS FERLKNLVAF LAKLMEKYEV ILVTSAAISA GHTKLDIDRK 

        70         80         90        100        110        120 
NLINKQVLAA IGQPFLISVY NELLAKFNKL GGQILLTGKD FDSRKATKHA KNAIDMMINL 

       130        140        150        160        170        180 
GILPIINEND ATAIEEIVFG DNDSLSAYAT HFFDADLLVI LSDIDGFYDK NPSEFSDAKR 

       190        200        210        220        230        240 
LEKITHIKEE WLQATIKTGS EHGTGGIVTK LKAAKFLLEH NKKMFLASGF DLSVAKTFLL 

       250 
EDKQIGGTLF E 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.
[2]"Crystal structure of glutamate 5-kinase from Campylobacter jejuni."
Gorman J., Shapiro L.
Submitted (AUG-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34268.1.
PIRA81426.
RefSeqYP_002343557.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AKOX-ray2.20A/B/C/D1-251[»]
ProteinModelPortalQ9PJ29.
SMRQ9PJ29. Positions 2-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9PJ29. 9 interactions.
STRING192222.Cj0097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL34268; CAL34268; Cj0097.
GeneID904426.
KEGGcje:Cj0097.
PATRIC20057121. VBICamJej33762_0095.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAALIICSD.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-93-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
HAMAPMF_00456. ProB.
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9PJ29.

Entry information

Entry namePROB_CAMJE
AccessionPrimary (citable) accession number: Q9PJ29
Secondary accession number(s): Q0PC40
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways