Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1JAG2 (PROB_STRPB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:MGAS2096_Spy1394
OrganismStreptococcus pyogenes serotype M12 (strain MGAS2096) [Complete proteome] [HAMAP]
Taxonomic identifier370553 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length275 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 – 275275Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000253004

Regions

Nucleotide binding180 – 1812ATP By similarity
Nucleotide binding222 – 2287ATP By similarity

Sites

Binding site171ATP By similarity
Binding site571Substrate By similarity
Binding site1441Substrate By similarity
Binding site1601Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1JAG2 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: CDD34990A2C098F0

FASTA27529,863
        10         20         30         40         50         60 
MGMMKRQFED VTRIVIKIGT SSLVLPTGKI NLEKIDQLAF VISSLMNKGK EVILVSSGAM 

        70         80         90        100        110        120 
GFGLDILKME KRPTNLAKQQ AVSSVGQVAM MSLYSQIFAH YQTNVSQILL TRDVVVFPES 

       130        140        150        160        170        180 
LANVTNAFES LISLGIVPIV NENDAVSVDE MDHATKFGDN DRLSAVVAGI TKADLLIMLS 

       190        200        210        220        230        240 
DIDGLFDKNP TIYEDAQLRS HVAVITQEII ASAGGAGSKF GTGGMLSKIQ SAQMVFENKG 

       250        260        270 
QMVLMNGANP RDILRVLEGQ PLGTWFKQIE EVTHD 

« 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: MGAS2096.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000261 Genomic DNA. Translation: ABF36446.1.
RefSeqYP_600990.1. NC_008023.1.

3D structure databases

ProteinModelPortalQ1JAG2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370553.MGAS2096_Spy1394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF36446; ABF36446; MGAS2096_Spy1394.
GeneID4066315.
KEGGspj:MGAS2096_Spy1394.
PATRIC19733317. VBIStrPyo133020_1426.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAIDGLYSC.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSPYO370553:GH2N-1462-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_STRPB
AccessionPrimary (citable) accession number: Q1JAG2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 56 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