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Q5E6W1 (PROB_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:VF_0740
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length369 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 – 369369Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109752

Regions

Domain277 – 35579PUA
Nucleotide binding170 – 1712ATP By similarity
Nucleotide binding212 – 2187ATP By similarity

Sites

Binding site111ATP By similarity
Binding site511Substrate By similarity
Binding site1381Substrate By similarity
Binding site1501Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E6W1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 511225B249E01CBB

FASTA36939,327
        10         20         30         40         50         60 
MNTQSQTIVV KLGTSVLTGG TLKLDRAHMV ELVRQCVQLK KAGHQVIVVT SGAIAAGREH 

        70         80         90        100        110        120 
LNYPELPKTM ANKQLLAAVG QSCLIQAWQS LFGIYGVDVG QMLLTRADLD DRERYLNARD 

       130        140        150        160        170        180 
MLQALLKNNI VPIVNENDAV ATNEIKVGDN DNLSALVGIL AGADKLLLLT DQSGLFTADP 

       190        200        210        220        230        240 
RKDPKAELIK EVHTIDETLR KIAGGSGTTL GTGGMATKLQ AADVARRAGI EVIIAAGSAE 

       250        260        270        280        290        300 
NVITDVVNSK PQGTKFLPVE CALESRKRWI LAGPPSKGSI VIDEGAVNAV QQKGSSLLSK 

       310        320        330        340        350        360 
GITEVSGHFV RGGVAKIVNT KGELIARGIS RYSSDDLSKI LGKHSQDIYA VLGYEYGPVA 


IHRDDLVLI 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW85235.1.
RefSeqYP_204123.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E6W1.
SMRQ5E6W1. Positions 5-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_0740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW85235; AAW85235; VF_0740.
GeneID3277856.
KEGGvfi:VF_0740.
PATRIC20112024. VBIVibFis127983_0733.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAFDAKEIP.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycAFIS312309:GIWP-775-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_VIBF1
AccessionPrimary (citable) accession number: Q5E6W1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 15, 2005
Last modified: May 14, 2014
This is version 62 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