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Q2S9T4 (PROB_HAHCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:HCH_05938
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

Protein attributes

Sequence length386 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 – 386386Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252981

Regions

Domain294 – 37279PUA
Nucleotide binding187 – 1882ATP By similarity

Sites

Binding site281ATP By similarity
Binding site681Substrate By similarity
Binding site1551Substrate By similarity
Binding site1671Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S9T4 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: EF6DBCA30D7695EA

FASTA38641,839
        10         20         30         40         50         60 
MSVRLQLGQL NESQARARLR ETRRWVIKIG SALLTNDGRG LALDAMGLWV DQLAALRKDG 

        70         80         90        100        110        120 
VEVVIVSSGA VAEGMSRLGW RERPKLLDEL QAAAAVGQMG LVQAWEAQFK RHGMQTAQIL 

       130        140        150        160        170        180 
LTHEDLSDRK RYLNARGALC TLIDMGVAPI INENDTVVTD EIRFGDNDTL AALVANLVEA 

       190        200        210        220        230        240 
DHLIILTDQS GLFDKDPRSN TDACLVGVAK ANDTALDSMA SGSSGALGRG GMFTKLRASR 

       250        260        270        280        290        300 
LASRSGAATV IVGGRIDSVL TRLRNGDELG TLLLPDQERW VARKQWLAGH LKTRGRLVLD 

       310        320        330        340        350        360 
DGAVRVLTQQ GRSLLPVGVK SVDGGFQRGE MVSCYDLQGN EVARGLVNYD ADEAVRIVGV 

       370        380 
ASEKIESILG YINEPELIHR DNLVML 

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KCTC 2396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000155 Genomic DNA. Translation: ABC32590.1.
RefSeqYP_437015.1. NC_007645.1.

3D structure databases

ProteinModelPortalQ2S9T4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349521.HCH_05938.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC32590; ABC32590; HCH_05938.
GeneID3842787.
KEGGhch:HCH_05938.
PATRIC22092104. VBIHahChe29232_5392.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycHCHE349521:GHAL-5735-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_HAHCH
AccessionPrimary (citable) accession number: Q2S9T4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 24, 2006
Last modified: June 11, 2014
This is version 62 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