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A8LK10 (PROB_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 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:Dshi_1467
OrganismDinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter

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_1000081055

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
A8LK10 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: D428AF8572887A65

FASTA36838,544
        10         20         30         40         50         60 
MATLSAARCL VVKIGSALLV DQASGALRQD WLTGLAQDVA EIRARGADVI LVSSGSIALG 

        70         80         90        100        110        120 
RRVLGLGTGA LPLEQAQAAA AVGQIRLARA YEEVLAPHKI TTAQVLVTLE DSTDRRRYLN 

       130        140        150        160        170        180 
TRATLGTLLS LGVTPIVNEN DTIATDEIRY GDNDRLAAQV AVMAGADQLV LLSDVDGLYT 

       190        200        210        220        230        240 
ANPATDPTAT RFDRVDEITP EIEAMAGDAV SGLSKGGMKT KLMAARTAMD AGCAMAITEG 

       250        260        270        280        290        300 
ARPRPLKALM DGAPATWFVP RTDPLAARKH WIAAMKPRGE ITVDAGACAA LKRGKSLLPA 

       310        320        330        340        350        360 
GITEVSGAFG RGDPVIILAP DGTALGRGLT RYTAVEARAI RGHRSAEIEA VLGYPGRAVL 


IHRDDMVL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000830 Genomic DNA. Translation: ABV93209.1.
RefSeqYP_001532810.1. NC_009952.1.

3D structure databases

ProteinModelPortalA8LK10.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398580.Dshi_1467.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV93209; ABV93209; Dshi_1467.
GeneID5712645.
KEGGdsh:Dshi_1467.
PATRIC21815541. VBIDinShi9476_1522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycDSHI398580:GKEL-1488-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_DINSH
AccessionPrimary (citable) accession number: A8LK10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: March 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