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A5CR33 (PROB_CLAM3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:CMM_1492
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP]
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length259 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 – 259259Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081050

Regions

Nucleotide binding173 – 1742ATP By similarity

Sites

Binding site181ATP By similarity
Binding site541Substrate By similarity
Binding site1411Substrate By similarity
Binding site1531Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CR33 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: CB591178832895AE

FASTA25926,711
        10         20         30         40         50         60 
MGTASRAGIA SARRIVVKVG SSSISGDNAG QIAPLVDAIA SVHARGAEVV LVSSGAIATG 

        70         80         90        100        110        120 
MPFLRLDDRP ADLATQQAAA AVGQSVLIFR YQESLDRYGI VAGQVLLTAG DLAAPDHREN 

       130        140        150        160        170        180 
AQRAMERLLG LRLLPIVNEN DTVATHEIRF GDNDRLAALV ARLVDADLLL LLSDVDALYT 

       190        200        210        220        230        240 
RPPEEPGARR IEHVGFGDEL DGVEIGSTGT GVGTGGAVTK VAAARLAAEA GTGVLLTSTA 

       250 
QVHSALAGEH VGTWFAPRG 

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCPPB 382.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM711867 Genomic DNA. Translation: CAN01538.1.
RefSeqYP_001222233.1. NC_009480.1.

3D structure databases

ProteinModelPortalA5CR33.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING443906.CMM_1492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAN01538; CAN01538; CMM_1492.
GeneID5175636.
KEGGcmi:CMM_1492.
PATRIC21453771. VBIClaMic82482_1605.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAALIICSD.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycCMIC443906:GCI2-1537-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.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePROB_CLAM3
AccessionPrimary (citable) accession number: A5CR33
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 45 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