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Q989S7 (PROB2_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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 2

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase 2
Short name=GK 2
Gene names
Name:proB2
Ordered Locus Names:mlr6298
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length284 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.

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

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 – 284284Glutamate 5-kinase 2 HAMAP-Rule MF_00456
PRO_0000109714

Regions

Nucleotide binding186 – 1872ATP By similarity
Nucleotide binding228 – 2347ATP By similarity

Sites

Binding site261ATP By similarity
Binding site671Substrate By similarity
Binding site1541Substrate By similarity
Binding site1661Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q989S7 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: C7E8BB7D23C4FA54

FASTA28430,683
        10         20         30         40         50         60 
MQEKIRETCL ATKTVKLLSA RRLIVKIGSA VVADAETGEI RGPWLETLIK DVVRFFARGQ 

        70         80         90        100        110        120 
QVIIVTSGAV AAGSRHFKQL DRSLRIEEKQ AAAAIGQIRL MIAYEQSLKR HGFGLGQVLL 

       130        140        150        160        170        180 
TSADVDNQRC RLNARSAFQQ LLNVGAVPVI NENDATATPE VCLGDNDRLA ARVAQIAKAD 

       190        200        210        220        230        240 
LLILLSDVDG LFTEDPHDNP LARMIPEVRR ITPEIEIMAS LSPARHGSGG MVTKLMAARI 

       250        260        270        280 
AMEAGCNVVI AKGSKSYPLA AIENGAPSTW FIPPARETAT RGGR 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB52617.1.
RefSeqNP_106831.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ989S7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr6298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB52617; BAB52617; BAB52617.
GeneID1229486.
KEGGmlo:mlr6298.
PATRIC22484243. VBIMesLot2464_5004.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAAQNAGCT.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-4979-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D3.40.1160.10. 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.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB2_RHILO
AccessionPrimary (citable) accession number: Q989S7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 70 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