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Q99YJ7 (PROB_STRP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:SPy_1672, M5005_Spy1371
OrganismStreptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]
Taxonomic identifier301447 [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_0000109734

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
Q99YJ7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6986C6CB586DB5A8

FASTA27329,756
        10         20         30         40         50         60 
MMKRQFEDVT RIVIKIGTSS LVLPTGKINL EKIDQLAFVI SSLMNKGKEV ILVSSGAMGF 

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

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

       190        200        210        220        230        240 
DGLFDKNPTI YEDAQLRSHV ANITQEIIAS AGGAGSKFGT GGMLSKVQSA QMVFENKGQM 

       250        260        270 
VLMNGANPRD ILRVLEGQPL GTWFKQIEEV RHD 

« Hide

References

[1]"Complete genome sequence of an M1 strain of Streptococcus pyogenes."
Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. expand/collapse author list , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.
Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700294 / SF370 / Serotype M1.
[2]"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004092 Genomic DNA. Translation: AAK34430.1.
CP000017 Genomic DNA. Translation: AAZ51989.1.
RefSeqNP_269709.1. NC_002737.1.
YP_282734.1. NC_007297.1.

3D structure databases

ProteinModelPortalQ99YJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160490.SPy_1672.

Proteomic databases

PaxDbQ99YJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK34430; AAK34430; SPy_1672.
AAZ51989; AAZ51989; M5005_Spy1371.
GeneID3571525.
901919.
KEGGspy:SPy_1672.
spz:M5005_Spy_1371.
PATRIC19716806. VBIStrPyo79812_1455.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAADDFDSR.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSPYO160490:GJ81-1381-MONOMER.
SPYO293653:GHFC-1442-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_STRP1
AccessionPrimary (citable) accession number: Q99YJ7
Secondary accession number(s): Q48XD6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 84 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