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Q04KZ3 (PROB_STRP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:SPD_0822
OrganismStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP]
Taxonomic identifier373153 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length369 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.

Contains 1 PUA domain.

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

RNA binding

Inferred from electronic annotation. Source: InterPro

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 – 369369Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081111

Regions

Domain275 – 35581PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site91ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04KZ3 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 3BFB8A045239C594

FASTA36939,883
        10         20         30         40         50         60 
MKYKRIVFKV GTSSLTNEDG SLSRSKVKDI TQQLAMLHEA GHELILVSSG AIAAGFGALG 

        70         80         90        100        110        120 
FKKRPTKIAD KQASAAVGQG LLLEEYTTNL LLRQIVSAQI LLTQDDFVDK RRYKNAHQAL 

       130        140        150        160        170        180 
SVLLNRGAIP IINENDSVVI DELKVGDNDT LSAQVAAMVQ ADLLVFLTDV DGLYTGNPNS 

       190        200        210        220        230        240 
DPRAKRLERI ETINREIIDM AGGAGSSNGT GGMLTKIKAA TIATESGVPV YICSSLKSDS 

       250        260        270        280        290        300 
MIEAAEETED GSYFVAQEKG LRTQKQWLAF YAQSQGSIWV DKGAAEALSQ HGKSLLLSGI 

       310        320        330        340        350        360 
VEAEGVFSYG DIVTVFDKES GKSLGKGRVQ FGASALEDIL RSQKAKGVLI YRDDWISITP 


EIQLLFTEF 

« Hide

References

[1]"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6."
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.
J. Bacteriol. 189:38-51(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D39 / NCTC 7466.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000410 Genomic DNA. Translation: ABJ55060.1.
RefSeqYP_816305.1. NC_008533.1.

3D structure databases

ProteinModelPortalQ04KZ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373153.SPD_0822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ55060; ABJ55060; SPD_0822.
GeneID4442275.
KEGGspd:SPD_0822.
PATRIC19682780. VBIStrPne27904_0927.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycSPNE373153:GIX6-822-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
3.40.1160.10. 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.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_STRP2
AccessionPrimary (citable) accession number: Q04KZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 51 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