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A3CMT0 (PROB_STRSV) 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:SSA_1072
OrganismStreptococcus sanguinis (strain SK36) [Complete proteome] [HAMAP]
Taxonomic identifier388919 [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_1000081113

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
A3CMT0 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: F60BDFFA6176CD36

FASTA36939,448
        10         20         30         40         50         60 
MKAKRIVFKV GTSSLTNADG SLSRAKVKEI TRQLALLHEA GHELILVSSG AIAAGFSSLG 

        70         80         90        100        110        120 
FKKRPTKVAD KQASAAVGQG LLLEEYTTNL LLKQIISAQI LLTQDDFADK RRYKNAHQAL 

       130        140        150        160        170        180 
SVLLNRGAIP IINENDTVAI EELKVGDNDT LSAQVAAMVQ ADLLVLLTDV DGLYTANPST 

       190        200        210        220        230        240 
NPDARRLEKI EKISSELIDM AGGAGTSNGT GGMLTKIKAA TLATMSGVPV YICSSLKSDA 

       250        260        270        280        290        300 
LLEAAEESKD GSLFLAQEKG LKTQKQWLAF YAKSQGEIYV DQGAADALRN NGKSLLVSGL 

       310        320        330        340        350        360 
VSVLGSFAYQ DTVTVYEDGS GAILGKGRVR FGKSSLKDML KSNKPKGVVI HRDDWISLTP 


ELNDLFAEF 

« Hide

References

[1]"Genome of the opportunistic pathogen Streptococcus sanguinis."
Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., Buck G.A.
J. Bacteriol. 189:3166-3175(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SK36.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000387 Genomic DNA. Translation: ABN44485.1.
RefSeqYP_001035035.1. NC_009009.1.

3D structure databases

ProteinModelPortalA3CMT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING388919.SSA_1072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN44485; ABN44485; SSA_1072.
GeneID4807235.
KEGGssa:SSA_1072.
PATRIC19769116. VBIStrSan33173_1019.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSSAN388919:GHEN-1057-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_STRSV
AccessionPrimary (citable) accession number: A3CMT0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 60 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