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Q8XHA6 (PROB_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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:CPE2579
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length269 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.

Sequence caution

The sequence CAD12651.1 differs from that shown. Reason: Frameshift at position 19.

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 – 269269Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109661

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
Q8XHA6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 985BB96992EFB8B4

FASTA26929,214
        10         20         30         40         50         60 
MRKALKDSKR IVVKVGTSTL TYENGSVNLM RIEKLSRVIS DICNMGKEVV LVSSGAIGVG 

        70         80         90        100        110        120 
VGKLRLEKKP ETIREKQAVA AVGQCALMHI YNKFFGEYSH VVAQVLLTRD VLENERMKNN 

       130        140        150        160        170        180 
VCNTFDTLLE KGIIPIVNEN DAISIDEIQN ILNFGDNDNL SAIVSTLVNA DTLIILSDID 

       190        200        210        220        230        240 
GFYDSDPRTN EDSKMLKEVY EITPEIEECA GGAGSNRGTG GMVTKLSAAK VATSNGIDMI 

       250        260 
LANGENPEIL IDILNGEDIG TMFVAKKGE 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the Clostridium perfringens genes involved in the adaptive response to oxidative stress."
Briolat V., Reysset G.
J. Bacteriol. 184:2333-2343(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 13 / Type A.
[2]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ420783 Genomic DNA. Translation: CAD12651.1. Frameshift.
BA000016 Genomic DNA. Translation: BAB82285.1.
RefSeqNP_563495.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XHA6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE2579.

Proteomic databases

PRIDEQ8XHA6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB82285; BAB82285; BAB82285.
GeneID990956.
KEGGcpe:CPE2579.
PATRIC19499253. VBICloPer59675_2651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAAYVATII.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycCPER195102:GJFM-2700-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_CLOPE
AccessionPrimary (citable) accession number: Q8XHA6
Secondary accession number(s): Q8VNV7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 77 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