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Q8DVN0 (PROB_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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:SMU_449
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length269 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 – 269269Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109731

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
Q8DVN0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 580E3DA5AB515525

FASTA26929,747
        10         20         30         40         50         60 
MNHMKRNFEH VKRIVIKIGT SSLVLPSGKI DLNKIDQLAF VISNLMNREL DVILVSSGAM 

        70         80         90        100        110        120 
GFGLDILKMD KRPAEVARQQ AVSSVGQVAM MSLYSQIFSH YQTNVSQILL TRDVVEFPES 

       130        140        150        160        170        180 
LENVTNTFET LLSMRIVPIV NENDAISVDE MDHTTKFGDN DRLSALVANI TNSDLLIMLS 

       190        200        210        220        230        240 
DIDGLFDKNP TIYDNAVLRE NVTEITEEIL KSAGGAGSKF GTGGMMSKIK SAQIIFDCDR 

       250        260 
QMILMNGANP RDILRALDGK MIGTLFAKE 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58199.1.
RefSeqNP_720893.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DVN0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58199; AAN58199; SMU_449.
GeneID1027960.
KEGGsmu:SMU_449.
PATRIC19663125. VBIStrMut61772_0395.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
KOK00931.
OMAAYVATII.
OrthoDBEOG6PGK7G.
ProtClustDBPRK12314.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-449-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_STRMU
AccessionPrimary (citable) accession number: Q8DVN0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 78 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