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Q5KYA3 (PROB_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:GK2048
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length374 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 – 374374Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109674

Regions

Domain276 – 35479PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site91ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5KYA3 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: D964FE8B4E68B89B

FASTA37440,081
        10         20         30         40         50         60 
MKRQRVVVKI GSSSLTDPKG GLCHDKLFDH VEAIAYLKQL GHDVILITSG AVAAGFGPLG 

        70         80         90        100        110        120 
YPARPTTIAG KQAAAAVGQS LLMQAYSSAF AQFGFTAAQL LLTRSDFYSR ERFRNLFATI 

       130        140        150        160        170        180 
TTLLENGAVP IINENDSVSI EELTFGDNDM LSALVAGFLH ADALILLTDI NGLYDANPKT 

       190        200        210        220        230        240 
NPQAKKYAFL PEITDEMIEA AGGIGSAVGT GGMRSKLLAA RKALSFGVSV FIGTGSGREK 

       250        260        270        280        290        300 
LADILAGKGD GTYIGVPFPK QMQMRKQWIA YHAPVAGMIT VDSGAEEALL MRGKSLLPAG 

       310        320        330        340        350        360 
VTAVSGDFHA MDVVDVVNEK GITIGRGQVY YAAADLKKVK GRPSEEARQY SYLHRPEVIH 

       370 
RDNWVTLRKE SVSK 

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000043 Genomic DNA. Translation: BAD76333.1.
RefSeqYP_147901.1. NC_006510.1.

3D structure databases

ProteinModelPortalQ5KYA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235909.GK2048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD76333; BAD76333; GK2048.
GeneID3184072.
KEGGgka:GK2048.
PATRIC21965485. VBIGeoKau81518_2198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycGKAU235909:GJO7-2136-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_GEOKA
AccessionPrimary (citable) accession number: Q5KYA3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 60 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