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C5CE10 (PROB_KOSOT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:Kole_1419
OrganismKosmotoga olearia (strain TBF 19.5.1) [Complete proteome] [HAMAP]
Taxonomic identifier521045 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeKosmotoga

Protein attributes

Sequence length359 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 – 359359Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000206272

Regions

Domain266 – 34378PUA
Nucleotide binding202 – 2087ATP By similarity

Sites

Binding site71ATP By similarity
Binding site471Substrate By similarity
Binding site1351Substrate By similarity
Binding site1471Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
C5CE10 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 43137309B2A700A7

FASTA35939,174
        10         20         30         40         50         60 
MAKITIKVGS NLLVQQDGQL DKRYIVELCR EIGNLMSEGH QVVLVSSGAR AAGYGYLNKS 

        70         80         90        100        110        120 
NAQEADLYMK QALCAVGQVQ LMKLYESAMS FYGIKVAQIL LTREDFSHRK RFLNLRNTLI 

       130        140        150        160        170        180 
GLTEMGILPI VNENDSVATE EIMFGDNDVL ASMFAIGWNA DYLLLMTSVD GVIDQNGKVI 

       190        200        210        220        230        240 
PFYREDTTNM AIAKNASSRW GSGGITSKIR AARAAAAAGI QTSICNGKKL ENIAQFVLTG 

       250        260        270        280        290        300 
QTGTVFERVG PIKAKKAWIG FLSKPKGSIF INEGAKIAIE NNRSLLPVGV VHIEGDFQAG 

       310        320        330        340        350 
DVVEIRLDDG TFLGKGIINF SSAEAKKIVG LKSDQLEDVL GYSCSKVLIH IDNLWKRDN 

« Hide

References

[1]"Complete sequence of Thermotogales bacterium TBF 19.5.1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Noll K.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TBF 19.5.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001634 Genomic DNA. Translation: ACR80112.1.
RefSeqYP_002941116.1. NC_012785.1.

3D structure databases

ProteinModelPortalC5CE10.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521045.Kole_1419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR80112; ACR80112; Kole_1419.
GeneID7968736.
KEGGkol:Kole_1419.
PATRIC22188130. VBIKosOle109242_1492.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycKOLE521045:GHRV-1452-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_KOSOT
AccessionPrimary (citable) accession number: C5CE10
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 34 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