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Q896G3 (PROB_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:CTC_01044
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length267 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 AAO35627.1 differs from that shown. Reason: Erroneous initiation.

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 – 267267Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109662

Regions

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

Sites

Binding site181ATP By similarity
Binding site581Substrate By similarity
Binding site1451Substrate By similarity
Binding site1571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q896G3 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: F6B2A67DEEC55699

FASTA26728,745
        10         20         30         40         50         60 
MQFNRKEYLK DVKNIVVKVG SSTLTYENGL LNLFHIEHLV RQLVDLHNRG YNVILVSSGA 

        70         80         90        100        110        120 
IGAGVGKLGL SEKPKSIPEK QAAAAVGQGI LLHTYEKIFA EYGKTIGQIL LTKEDMIDEV 

       130        140        150        160        170        180 
RSCNATNTFN ALLDKRVIPI INENDAVVVD EIKVGDNDTL SAFVSKLVKA DLLILMSDIE 

       190        200        210        220        230        240 
GLYSCDPRIN NDAELINFVE KITKDIISCA GGAGTDLGTG GMATKIKAAK IATSAGIPML 

       250        260 
IVNGATNEVL QDVVEGKSVG TWFNAIK 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO35627.1. Different initiation.
RefSeqNP_781690.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ896G3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC01044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO35627; AAO35627; CTC_01044.
GeneID1059732.
KEGGctc:CTC01044.
PATRIC19509955. VBICloTet101274_1026.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
KOK00931.
OMAAYVATII.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycCTET212717:GJAM-955-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_CLOTE
AccessionPrimary (citable) accession number: Q896G3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 72 of the entry and version 2 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