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Q1JFK5 (PROB_STRPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:MGAS10270_Spy1489
OrganismStreptococcus pyogenes serotype M2 (strain MGAS10270) [Complete proteome] [HAMAP]
Taxonomic identifier370552 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length273 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.

Sequence caution

The sequence ABF34554.1 differs from that shown. Reason: Erroneous initiation.

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 – 273273Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000253006

Regions

Nucleotide binding178 – 1792ATP By similarity
Nucleotide binding220 – 2267ATP By similarity

Sites

Binding site151ATP By similarity
Binding site551Substrate By similarity
Binding site1421Substrate By similarity
Binding site1581Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1JFK5 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: B0E60737FD3B9B06

FASTA27329,702
        10         20         30         40         50         60 
MMKRQFEDVT RIVIKIGTSS LVLPTGKINL EKIDQLAFVI SSLMNKGKEV ILVSSGAMGF 

        70         80         90        100        110        120 
GLDILKMEKR PTNLAKQQAV SSVGQVAMMS LYSQIFAHYQ TNVSQILLTR DIVVFPESLA 

       130        140        150        160        170        180 
NVTNAFESLI SLGIVPIVNE NDAVSVDEMD HATKFGDNDR LSAVVAGITK ADLLIMLSDI 

       190        200        210        220        230        240 
DGLFDKSPTI YEDAQLRSHV AVITQEIIAS AGGAGSKFGT GGMLSKVQSA QMVFENKGQM 

       250        260        270 
VLMNGANPRD ILRVLEGQPL GTWFKQIEEV RHD 

« Hide

References

[1]"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus."
Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS10270.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000260 Genomic DNA. Translation: ABF34554.1. Different initiation.
RefSeqYP_599098.1. NC_008022.1.

3D structure databases

ProteinModelPortalQ1JFK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370552.MGAS10270_Spy1489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF34554; ABF34554; MGAS10270_Spy1489.
GeneID4064104.
KEGGsph:MGAS10270_Spy1489.
PATRIC19720942. VBIStrPyo120482_1516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSPYO370552:GHYF-1556-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 namePROB_STRPD
AccessionPrimary (citable) accession number: Q1JFK5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 57 of the entry and version 2 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