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B2UCV2 (PROB_RALPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Rpic_3064
OrganismRalstonia pickettii (strain 12J) [Complete proteome] [HAMAP]
Taxonomic identifier402626 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length374 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 – 374374Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000125251

Regions

Domain282 – 36079PUA
Nucleotide binding175 – 1762ATP By similarity

Sites

Binding site161ATP By similarity
Binding site561Substrate By similarity
Binding site1431Substrate By similarity
Binding site1551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B2UCV2 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 5270A7805FB3C13D

FASTA37439,356
        10         20         30         40         50         60 
MALHSLIADA RRLVVKVGSS LVTNDGRGLD QAAIARWAAQ IAALRAAGKE VVLVSSGAIA 

        70         80         90        100        110        120 
EGMQRLGWAK RPKEIHELQA AAAVGQMGLA QVYESEFARH SIRTAQVLLT HGDLADRERY 

       130        140        150        160        170        180 
LNARSTLLTL LSLGVVPIIN ENDTVVTDEI KFGDNDTLGA LVTNLIEGDA LIILTDQRGL 

       190        200        210        220        230        240 
YTADPRKDPG ARFVDEAQAG TPDLEQMAGG AGSSIGKGGM LTKILAAKRA AKSGAHTIIA 

       250        260        270        280        290        300 
SGREADVLAR LASGEAIGTQ LRAPTGRMAA RKQWMIDHLQ LRGRVVLDAG AVEKLTAGGK 

       310        320        330        340        350        360 
SLLPIGVTEV QGEFARGEVI SCVDAAGLEV ARGLTNYSSA EARLIARKAS SEIEAVLGYV 

       370 
SAAELVHRDN LVLL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia pickettii 12J."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marsh T., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001068 Genomic DNA. Translation: ACD28187.1.
RefSeqYP_001900619.1. NC_010682.1.

3D structure databases

ProteinModelPortalB2UCV2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402626.Rpic_3064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD28187; ACD28187; Rpic_3064.
GeneID6289009.
KEGGrpi:Rpic_3064.
PATRIC20256937. VBIRalPic63053_4201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycRPIC402626:GH94-3103-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_RALPJ
AccessionPrimary (citable) accession number: B2UCV2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 43 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