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Q7NPI6 (PROB_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. 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:gll0069
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

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_0000109676

Regions

Domain275 – 35379PUA
Nucleotide binding167 – 1682ATP By similarity
Nucleotide binding208 – 2147ATP By similarity

Sites

Binding site71ATP By similarity
Binding site481Substrate By similarity
Binding site1351Substrate By similarity
Binding site1471Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NPI6 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 98B51CA99F8DC482

FASTA36938,985
        10         20         30         40         50         60 
MVALVVKIGT SSLSDPSTGD LRLATLGGLA ETLTRLRRAG HRIILVSSGA VGVGCARLGL 

        70         80         90        100        110        120 
KERPATVAGK QAAAAVGQGL LMSMYDRLFG ALGQPVAQVL LTRQDLMDRV RYLNARETLS 

       130        140        150        160        170        180 
ELWRLGTVPI VNENDTVATD ELRFGDNDAL SALVAGLVEA QWLVLLTDVA GLYSANPRLD 

       190        200        210        220        230        240 
PQARLLSEVT EISEELLQSA RGRSLWGSGG MASKLEAARI AASAGVATVI TEGNTPQNIE 

       250        260        270        280        290        300 
RILAGEAIGT RFALARPGGR LSLRKRWIGY GLVPAGALHL DEGAVLAVRE GGKSLLPAGV 

       310        320        330        340        350        360 
RGVEGRFETG ALVRLIDGQG LEFARGLVNY SSEELEKIRG RKSHEIAALL GIEGQPPTAV 


HRDNLVTLS 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC88010.1.
RefSeqNP_923015.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NPI6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gvip004.

Proteomic databases

PRIDEQ7NPI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC88010; BAC88010; BAC88010.
GeneID2600046.
KEGGgvi:gvip004.
PATRIC22039487. VBIGloVio86258_0072.

Phylogenomic databases

eggNOGCOG0263.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.
PhylomeDBQ7NPI6.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-69-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_GLOVI
AccessionPrimary (citable) accession number: Q7NPI6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 72 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