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Q5LRY5 (PROB_RUEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:SPO1985
OrganismRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length368 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 – 368368Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109726

Regions

Domain278 – 35578PUA
Nucleotide binding173 – 1742ATP By similarity

Sites

Binding site131ATP By similarity
Binding site541Substrate By similarity
Binding site1411Substrate By similarity
Binding site1531Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LRY5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: B47E60844D0CA8F2

FASTA36838,548
        10         20         30         40         50         60 
MATLTTARRL VVKIGSALLV DRNTGDLRAD WLHSLAADVA WLKGLGLDVI LVSSGSIALG 

        70         80         90        100        110        120 
RGVLGLPRTA LPLEQSQAAA AVGQIRLARA YEEALAPHRI TTAQVLVTLE DSEDRRRYLN 

       130        140        150        160        170        180 
SRATLETLLG LGAVPIVNEN DTVATDEIRY GDNDRLAAQI AVTVGADQLI LLSDVDGFYT 

       190        200        210        220        230        240 
GNPSDDPGAT RFDVIDRITP EIVAMAGDAG SGLSKGGMKT KLMAAQMATA GGCAMAITEG 

       250        260        270        280        290        300 
SPLNPLKTLE NGANCTWFTA TLDPQAARKR WIAAMKPRGD ITVDAGAARA LEGGKSLLPA 

       310        320        330        340        350        360 
GVASVTGDFG RGDPVAILGP DGRRLGQGLC RYTGDEARAI RGRQSSDIEA TLGYPGRAAL 


IHRDDMAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV95261.1.
RefSeqYP_167220.1. NC_003911.12.

3D structure databases

ProteinModelPortalQ5LRY5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246200.SPO1985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV95261; AAV95261; SPO1985.
GeneID3193117.
KEGGsil:SPO1985.
PATRIC23377301. VBIRuePom114501_2011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAIDGLYSC.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

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_RUEPO
AccessionPrimary (citable) accession number: Q5LRY5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 65 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