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Q39QR3 (PROB_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:Gmet_3198
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length373 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 – 373373Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230046

Regions

Domain281 – 35979PUA
Nucleotide binding174 – 1752ATP By similarity
Nucleotide binding216 – 2227ATP By similarity

Sites

Binding site151ATP By similarity
Binding site551Substrate By similarity
Binding site1421Substrate By similarity
Binding site1541Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39QR3 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: F9B4E9117C0761B3

FASTA37340,358
        10         20         30         40         50         60 
MRTAILKKVK RIVIKIGSRV LTGDENGLNH AFIARLAAET ASLRQQGRQV IVVSSGAVAA 

        70         80         90        100        110        120 
GRRELGIEGR PKSIPQKQAA AAIGQSRLMR AYEEDFGRFG HKVAQILLTR DDLANRRRFL 

       130        140        150        160        170        180 
NARATLDTLL DFGVIPVINE NDTVVVDEIK FGDNDNLSAL VTNLAEAHLL VILTDIDGFY 

       190        200        210        220        230        240 
DSDPRANPDA RLIHLVKSIT RETERAAGDS GSSVGTGGMV TKLAAAKKAG QFGVPTLMLN 

       250        260        270        280        290        300 
GTVPGILTKA FAGREVGTLF LPARESLNRR KHWIAHTLRP SGRVIVDDGA RTVLSRQGKS 

       310        320        330        340        350        360 
LLPSGVIRVE GEFDRGACVR VCGADGAEIA RGVVDYSHAE IERILGHRSG EIEAILGYKY 

       370 
GDEIIHRDNL VVL 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB33411.1.
RefSeqYP_006722153.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39QR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269799.Gmet_3198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB33411; ABB33411; Gmet_3198.
GeneID3741108.
KEGGgme:Gmet_3198.
PATRIC22005656. VBIGeoMet55070_3234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMARLMRAYE.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycGMET269799:GHNY-3243-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_GEOMG
AccessionPrimary (citable) accession number: Q39QR3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 64 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