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Q8NZX8 (PROB_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:spyM18_1681
OrganismStreptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]
Taxonomic identifier186103 [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.

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_0000109737

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
Q8NZX8 [UniParc].

Last modified October 10, 2002. Version 1.
Checksum: EA26A7A28B001570

FASTA27329,660
        10         20         30         40         50         60 
MMKRQFEDVT RIVIKIGTSS LVLPTGKINL EKIDQLAFVI SSLMNKGKEV ILVSSGAMGF 

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

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

       190        200        210        220        230        240 
DGLFDKNPTI YEDAQLRSHV AVVTQEIIAS AGGAGSKFGT GGMLSKIQSA QMVFENKGQM 

       250        260        270 
VLMNGANPRD ILRVLEGQPL GTWFKQIEEV THD 

« Hide

References

[1]"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009949 Genomic DNA. Translation: AAL98221.1.
RefSeqNP_607722.1. NC_003485.1.

3D structure databases

ProteinModelPortalQ8NZX8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186103.spyM18_1681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL98221; AAL98221; spyM18_1681.
GeneID994584.
KEGGspm:spyM18_1681.
PATRIC19749862. VBIStrPyo4396_1505.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAAYVATII.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycSPYO186103:GHJG-1451-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_STRP8
AccessionPrimary (citable) accession number: Q8NZX8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: February 19, 2014
This is version 72 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