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Q2K2X5 (PROB_RHIEC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:
Glutamate 5-kinase

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase
Short name=GK
Gene names
Name:proB
Ordered Locus Names:RHE_CH04068
OrganismRhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]
Taxonomic identifier347834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Contains 1 PUA domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete 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

RNA binding

Inferred from electronic annotation. Source: InterPro

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 – 389389Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252992

Regions

Domain281 – 35878PUA
Nucleotide binding175 – 1762ATP By similarity

Sites

Binding site161ATP By similarity
Binding site561Substrate By similarity
Binding site1431Substrate By similarity
Binding site1551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2K2X5 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 568FDAF463D7983B

FASTA38940,909
        10         20         30         40         50         60 
MTSRKPLGRY RRIVIKIGSA LLVDRKAGLK KAWLDAMCAD IAGLKARGID VLVVSSGAIA 

        70         80         90        100        110        120 
LGRSVLDLPS GALKLEESQA AAAVGQIALA RAWSESLSRD EIVAGQILLT LGDTEERRRY 

       130        140        150        160        170        180 
LNARATINQL LKIGAVPIIN ENDTVATSEI RYGDNDRLAA RVATMTGADL LILLSDIDGL 

       190        200        210        220        230        240 
YTAPPHLDPN ATFLETISEI TPEIEAMAGG AASELSRGGM RTKIDAGKIA TTSGCAMIIA 

       250        260        270        280        290        300 
SGKTESPLSA IENGARSSWF APSGTPVTAR KTWIAGQLQP AGELHVDEGA VTALGAGKSL 

       310        320        330        340        350        360 
LPAGLRSVSG LFSRGDTVAI IGPAGREIAR GLVSYDAEDA RRIAGRKSAE IEAILGYAGR 

       370        380 
AAMVHRDDMV MTAQIRPKSE RQKKDASYA 

« Hide

References

[1]"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons."
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFN 42 / ATCC 51251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000133 Genomic DNA. Translation: ABC92811.1.
RefSeqYP_471538.1. NC_007761.1.

3D structure databases

ProteinModelPortalQ2K2X5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347834.RHE_CH04068.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC92811; ABC92811; RHE_CH04068.
GeneID3894067.
KEGGret:RHE_CH04068.
PATRIC23089886. VBIRhiEtl108884_4575.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycRETL347834:GJJ0-4086-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
3.40.1160.10. 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.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_RHIEC
AccessionPrimary (citable) accession number: Q2K2X5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 56 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