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Q2S355 (PROB_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:SRU_1252
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length376 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
Reference 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 – 376376Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000253000

Regions

Domain280 – 36182PUA
Nucleotide binding173 – 1742ATP By similarity
Nucleotide binding215 – 2217ATP By similarity

Sites

Binding site151ATP By similarity
Binding site551Substrate By similarity
Binding site1411Substrate By similarity
Binding site1531Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S355 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: B43C4CD281DD3A15

FASTA37640,118
        10         20         30         40         50         60 
MATVALPDWT RAVVKVGSAL VAPDDRGCST THLLPIARFV IQSRRQGKEV ILVSSGAVAA 

        70         80         90        100        110        120 
GLAEQGRGGP GTGLSIPERQ ALAALGQPLL MAHWRRLFDV PCAQVLLTYD DLQRRARFVN 

       130        140        150        160        170        180 
AKNTIAELLD RDTLPIVNEN DTVATEELRV GDNDNLAAYV AVLAEADLLV ICSDVDGLYT 

       190        200        210        220        230        240 
ADPHDDPDAE RLPAVDAITD EIYDMVGPSH RKVATGGMQT KVEAAEKATD RGIDTVLVNG 

       250        260        270        280        290        300 
TKGGHLDALG RGEMPGTLFR QAEQPLPARK HWMLHALPSA GRLTVDAGAA DALRHEGASL 

       310        320        330        340        350        360 
LPSGIVAVEG RFARGDAVEI AVEKEGNRTR VAKGITQYGA ADLERIQGRQ SHAIAEVLDE 

       370 
APADYVVHRD DLVVEA 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC44492.1.
RefSeqYP_445376.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_1252.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC44492; ABC44492; SRU_1252.
GeneID3851194.
KEGGsru:SRU_1252.
PATRIC23424917. VBISalRub86502_1298.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAHIANGKT.
OrthoDBEOG6PGK7G.
PhylomeDBQ2S355.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-1249-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.
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.
PROSITEPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_SALRD
AccessionPrimary (citable) accession number: Q2S355
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 67 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