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Q48RY6 (PROB_STRPM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:M28_Spy1414
OrganismStreptococcus pyogenes serotype M28 (strain MGAS6180) [Complete proteome] [HAMAP]
Taxonomic identifier319701 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length272 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 AAX72524.1 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 – 272272Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230069

Regions

Nucleotide binding177 – 1782ATP By similarity
Nucleotide binding219 – 2257ATP By similarity

Sites

Binding site141ATP By similarity
Binding site541Substrate By similarity
Binding site1411Substrate By similarity
Binding site1571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48RY6 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 371625F1BC65AAF2

FASTA27229,543
        10         20         30         40         50         60 
MKRQFEDVTR IVIKIGTSSL VLPTGKINLE KIDQLAFVIS SLMNKGKEVI LVSSGAMGFG 

        70         80         90        100        110        120 
LDILKMEKRP TNLAKQQAVS SVGQVAMMSL YSQIFAHYQT NVSQILLTRD VVVFPESLAN 

       130        140        150        160        170        180 
VTNAFESLIS LGIVPIVNEN DAVSVDEMDH ATKFGDNDRL SAVVAGITKA DLLIMLSDID 

       190        200        210        220        230        240 
GLFDKNPTIY EDAQLRSHVA VITQEIIASA GGAGSKFGTG GMLSKIQSAQ MVFENKGQMV 

       250        260        270 
LMNGANPRDI LRVLEGQPLG TWFKQIEEVT HD 

« Hide

References

[1]"Genome sequence of a serotype M28 strain of group A Streptococcus: potential new insights into puerperal sepsis and bacterial disease specificity."
Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B., Lefebvre R.B., Musser J.M.
J. Infect. Dis. 192:760-770(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS6180.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000056 Genomic DNA. Translation: AAX72524.1. Different initiation.
RefSeqYP_280879.1. NC_007296.1.

3D structure databases

ProteinModelPortalQ48RY6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319701.M28_Spy1414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX72524; AAX72524; M28_Spy1414.
GeneID3574134.
KEGGspb:M28_Spy1414.
PATRIC19745663. VBIStrPyo35950_1450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSPYO319701:GHAD-1479-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_STRPM
AccessionPrimary (citable) accession number: Q48RY6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: May 14, 2014
This is version 60 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