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Q2L067 (PROB_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:BAV0256
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length377 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 – 377377Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252971

Regions

Domain284 – 36279PUA
Nucleotide binding177 – 1782ATP By similarity
Nucleotide binding219 – 2257ATP By similarity

Sites

Binding site181ATP By similarity
Binding site581Substrate By similarity
Binding site1451Substrate By similarity
Binding site1571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2L067 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 972C180FEED79088

FASTA37740,201
        10         20         30         40         50         60 
MTASPISVIA SANRLVAKVG SSLVTNEGRG LDRAAVAHWA AQIAALHKQG RQVVLVSSGA 

        70         80         90        100        110        120 
IAEGMARLGW RKRPSVMHEL QAAAAVGQMG LCQAYEAAFA EHGLRTAQIL LTHEDLADRH 

       130        140        150        160        170        180 
RYLNARSTLF ALLRMGVVPI VNENDTVVTD EIRLGDNDTL GALVTNLIEA DSLIILTDQR 

       190        200        210        220        230        240 
GLYEADPRKN PDARFISHAQ AGDTALEAMA GGAGSGVGTG GMLTKILAAK RAAHSGAHTV 

       250        260        270        280        290        300 
IASGRERNVL TRLAQGECIG TELQATLPVW SARKQWMADH LRLRGRLVLD EGAVQALLNE 

       310        320        330        340        350        360 
GKSLLPIGVT EVQGDFERGD VVACVDASGR ECARGLVNYA SADARRIMRH PSSEITQILG 

       370 
SMTAPELMHR DNLVITE 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ47861.1.
RefSeqYP_784794.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L067.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV0256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6264596.
KEGGbav:BAV0256.
PATRIC21126656. VBIBorAvi43433_0269.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAIDGLYSC.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycBAVI360910:GCKI-260-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_BORA1
AccessionPrimary (citable) accession number: Q2L067
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 59 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