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Q2VZU1 (PROB_MAGSA) 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:amb4080
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length370 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 – 370370Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252984

Regions

Domain278 – 35578PUA
Nucleotide binding172 – 1732ATP By similarity
Nucleotide binding214 – 2207ATP By similarity

Sites

Binding site131ATP By similarity
Binding site541Substrate By similarity
Binding site1401Substrate By similarity
Binding site1521Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2VZU1 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: D0DD407A1BB7E11C

FASTA37039,445
        10         20         30         40         50         60 
MSPLAAAKRL IVKIGSSLLV DDSTGQVRRG WLETLAADIA ACKARGQEVI VVSSGAVAVG 

        70         80         90        100        110        120 
RRKLGLVPPL KLEEKQAAAA TGQIRLAHAW QDALAHHQIT VAQVLLTLDD SENRRRYLNA 

       130        140        150        160        170        180 
RSTLETLLKL GAVPVINEND TVATAEIRVG DNDRLAARVA QMVSADALVL FSDIDGLYTA 

       190        200        210        220        230        240 
DPRKDPDARF IPEVHELTPE IEAMAGDPGS AYGSGGMVTK LVAARICLSA GCRMAITRGE 

       250        260        270        280        290        300 
PMHPLKTIED GGRCTWFLPN SEPRTARKQW IFGSMKPTGT LVLDAGAARA LAQGRSLLPA 

       310        320        330        340        350        360 
GITEVSGAFE RGDCVLVKDG SGKVLGRGLV AYSADDSRAI MGRKSGEIEA ILGFRGRDEL 

       370 
IHRDDLVMEG 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE52884.1.
RefSeqYP_423443.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2VZU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342108.amb4080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE52884; BAE52884; amb4080.
GeneID3803118.
KEGGmag:amb4080.
PATRIC22442468. VBIMagMag129836_4053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-4129-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_MAGSA
AccessionPrimary (citable) accession number: Q2VZU1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 10, 2006
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