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C1L2G8 (PROB_LISMC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Lm4b_01270
OrganismListeria monocytogenes serotype 4b (strain CLIP80459) [Complete proteome] [HAMAP]
Taxonomic identifier568819 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length276 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.

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

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 – 276276Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000206273

Regions

Nucleotide binding177 – 1782ATP By similarity
Nucleotide binding219 – 2257ATP By similarity

Sites

Binding site141ATP By similarity
Binding site541Substrate By similarity
Binding site1411Substrate By similarity
Binding site1571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
C1L2G8 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: EFEFA99B7FFD91A4

FASTA27630,032
        10         20         30         40         50         60 
MRESLKNSKR LVIKVGTSTL MYGNGHINLR TIEKLAMVLS DLRNEGKEVI LVSSGAIGVG 

        70         80         90        100        110        120 
CHKLQLSVRP TSIPDLQAVA SVGQSELMHI YSKFFGEYGQ VVGQVLLTRD VTDFPISREN 

       130        140        150        160        170        180 
VMNTLDSLLS RGIIPIVNEN DTVAVEELEH VTKYGDNDLL SAIVAKLVQA DLLIMLSDID 

       190        200        210        220        230        240 
GFYGSNPATD PEAVMFSEIN QITPEIEALA GGRGSKFGTG GMLTKLSAAS YCMDSNQKMI 

       250        260        270 
LTNGKNPTVI FNIMQGEQIG TLFASKKEEL SHDRTH 

« Hide

References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIP80459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM242711 Genomic DNA. Translation: CAS05034.1.
RefSeqYP_002757970.1. NC_012488.1.

3D structure databases

ProteinModelPortalC1L2G8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634178.Lm4b_01270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS05034; CAS05034; Lm4b_01270.
GeneID7704070.
KEGGlmc:Lm4b_01270.
PATRIC20305702. VBILisMon88360_1278.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246368.
KOK00931.
OMAAYVATII.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycLMON568819:GJF9-1888-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...

Entry information

Entry namePROB_LISMC
AccessionPrimary (citable) accession number: C1L2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 36 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