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Q8G4T9 (PROB_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:BL1285
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

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
Reference 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_0000109646

Regions

Domain285 – 36379PUA
Nucleotide binding181 – 1822ATP By similarity
Nucleotide binding223 – 2297ATP 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
Q8G4T9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2196B4E8563223FA

FASTA37739,188
        10         20         30         40         50         60 
MSTPSQAEVR RMIAAAGTIV VKVGSSSLTQ PSGHLDPDKL DALAAALAQV RLMGGRVVLV 

        70         80         90        100        110        120 
SSGAIAAGFG PLGFDSRPVD VATQQATAAV GQGLLMARYE TAFGRFGIRV GQILITAEDT 

       130        140        150        160        170        180 
IRATQYRNVE RTLDRLLDLG VVPIINENDS LASNEIRFGD NDRLSALVAN LVRAEALVLL 

       190        200        210        220        230        240 
TDVDALYTAP PSQPGSRRVE YVPNVIDALG DIQVSGSGSK VGTGGMVTKL EAARVAAVSG 

       250        260        270        280        290        300 
IPTVLTCASN AGPAMMGDPV GTVFAPVKAR GSSRRLWIGF AADPRGTIVV DAGAGQAIRG 

       310        320        330        340        350        360 
GRASLLAAGA LEVHGDFSAG DPVWIDAESG EHLARGLAGF DSEEIPQMLG RNTAQLKRFL 

       370 
GPQYAHPLVH RDNLVLV 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN25086.1.
RefSeqNP_696450.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G4T9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL1285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN25086; AAN25086; BL1285.
GeneID1023196.
KEGGblo:BL1285.
PATRIC21120272. VBIBifLon107831_1572.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAHGEISIR.
OrthoDBEOG6PGK7G.
PhylomeDBQ8G4T9.

Enzyme and pathway databases

BioCycBLON206672:GI1E-1499-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_BIFLO
AccessionPrimary (citable) accession number: Q8G4T9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 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