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Q28Q11 (PROB_JANSC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:Jann_2284
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length368 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 – 368368Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252982

Regions

Domain278 – 35578PUA
Nucleotide binding173 – 1742ATP By similarity

Sites

Binding site131ATP By similarity
Binding site541Substrate By similarity
Binding site1411Substrate By similarity
Binding site1531Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28Q11 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 80E477F24942CB87

FASTA36837,655
        10         20         30         40         50         60 
MASLTGAKRV VVKIGSALLV DRHTGDLRAD WLAALADDIA ALKGAGTDVI LVSSGAIALG 

        70         80         90        100        110        120 
RGVLALGDGA LSLDEAQAAA AVGQIRLARA YEEVLAPLGL TSAQILLTLD DSADRRRYLN 

       130        140        150        160        170        180 
TRATFAALLA RGAVPIVNEN DTIATDEIRY GDNDRLAANV AVMAGADICV LLSDVDGLYT 

       190        200        210        220        230        240 
ANPNDDTTAA HLPVIDTITP EIEAMAGDAG SGLSKGGMKT KVLAARTATA AGCAMAITQG 

       250        260        270        280        290        300 
AIANPLRALD DGARATWFTA TVSPQQARKA WIGAMKPKGS LRLDAGAAAA LSRGKSLLPA 

       310        320        330        340        350        360 
GVVAVTGDFL RGDPVRLEAP DGAAIGIGLS RYGAKEALAI QGHQSDEIPE ILGYPGRAAL 


VHRDDMVL 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000264 Genomic DNA. Translation: ABD55201.1.
RefSeqYP_510226.1. NC_007802.1.

3D structure databases

ProteinModelPortalQ28Q11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290400.Jann_2284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD55201; ABD55201; Jann_2284.
GeneID3934740.
KEGGjan:Jann_2284.
PATRIC22148332. VBIJanSp43325_2429.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAIDGLYSC.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycJSP290400:GI1R-2304-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_JANSC
AccessionPrimary (citable) accession number: Q28Q11
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 4, 2006
Last modified: May 14, 2014
This is version 57 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