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Q6G0S7 (PROB_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:BQ01470
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length384 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 – 384384Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109645

Regions

Domain287 – 36478PUA
Nucleotide binding181 – 1822ATP By similarity

Sites

Binding site221ATP By similarity
Binding site621Substrate By similarity
Binding site1491Substrate By similarity
Binding site1611Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G0S7 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 9748629150530C8E

FASTA38441,208
        10         20         30         40         50         60 
MSGLIKTAGL QKLAHYKRIV VKIGSALLVE PQTGLRAEWL KSLINDVAKL HQKGVEILLV 

        70         80         90        100        110        120 
SSGAIALGRT LLRLPRGALK LEESQACAAL GQIELAKTYG DALAQYGLKT GQILLTLLDT 

       130        140        150        160        170        180 
EERRRYLNAR ATINVLLRFG AVPVINENDT VATSEIRYGD NDRLAARVAT MMGADLLILL 

       190        200        210        220        230        240 
SDIDGLYTKS PHRDPTAEFI PFIASITSDI EKMADVAASE LSRGGMKTKL DAGKIANSAG 

       250        260        270        280        290        300 
TAMVITSGKR MNPLAAIDRG ERRSFFAASE KPVNAWKTWI SGHLGPSGIL TIDPGAAKAL 

       310        320        330        340        350        360 
ESGKSLLAAG VIAVDGMFHR GDTVAIVDTN GVEIARGLVS YGKNEAVRIM GCKREEIESI 

       370        380 
LGYEARSAMV HRNDMVLRCL TDST 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF25650.1.
RefSeqYP_031859.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6G0S7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ01470.

Proteomic databases

PRIDEQ6G0S7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF25650; CAF25650; BQ01470.
GeneID2867517.
KEGGbqu:BQ01470.
PATRIC31951457. VBIBarQui58630_0168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycBQUI283165:GHZA-147-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_BARQU
AccessionPrimary (citable) accession number: Q6G0S7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 69 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