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Reviewed, UniProtKB/Swiss-Prot A9IFG1 (PROB_BORPD)

Last modified November 3, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Bpet4680
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP MF_00456

Subcellular location

Cytoplasm By similarity.

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 processproline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Glutamate 5-kinase HAMAP MF_00456
PRO_1000125214

Regions

Domain286 – 36479PUA

Sequences

Sequence LengthMass (Da)Tools
A9IFG1-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: B00B18FE3003F756

FASTA37840,246
        10         20         30         40         50         60 
MTADTTAVSV VASATRLVAK VGSSLVTNEG RGLDRAAVAH WAAQIAALRQ QGKQVVLVSS 

        70         80         90        100        110        120 
GAIAEGMARL GWRKRPSVMH ELQAAAAVGQ MGLCQAYEAA FAEHGLRTAQ ILLTHEDLAD 

       130        140        150        160        170        180 
RHRYLNARST LFALMRLGVV PIVNENDTVV TDEIRLGDND TLGALVTNLI EADALVILTD 

       190        200        210        220        230        240 
QRGLYDSDPR KNPDAVFVAH AQAGDPELEA MAGGAGSGIG TGGMLTKILA AKRAAHSGAH 

       250        260        270        280        290        300 
TVIASGRERN VLTRLAQGEC IGTELRAVLP VWSARKQWLA DHLRLRGRVV LDAGAVRALL 

       310        320        330        340        350        360 
HEGKSLLPIG VIDVQGEFER GDVVACIDPQ GAECARGLIN YSSADTRRIL RQPSSQIARI 

       370 
LGSMTDPELM HRDNLVVI 

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM902716 Genomic DNA. Translation: CAP45031.1.
RefSeqYP_001633298.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5818761.
GenomeReviewsGene locus Bpet4680 in contig AM902716_GR.
KEGGbpt:Bpet4680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAILTDQRG.

Family and domain databases

HAMAPMF_00456.
[Tree]
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu_5kinase.
IPR011529. Glu_5kinase_bact.
IPR019797. Glutamate_5-kinase_CS.
IPR005715. ProB.
IPR002478. PUA.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_BORPD
AccessionPrimary (citable) accession number: A9IFG1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents