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Q57ST3 (PROB_SALCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:SCH_0322
OrganismSalmonella choleraesuis (strain SC-B67) [Complete proteome] [HAMAP]
Taxonomic identifier321314 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length367 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 – 367367Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109719

Regions

Domain275 – 35379PUA
Nucleotide binding169 – 1702ATP By similarity
Nucleotide binding211 – 2177ATP By similarity

Sites

Binding site101ATP By similarity
Binding site501Substrate By similarity
Binding site1371Substrate By similarity
Binding site1491Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57ST3 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: D3EBCD6AB89DEDF8

FASTA36739,141
        10         20         30         40         50         60 
MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS GAIAAGREHL 

        70         80         90        100        110        120 
GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHIGQ MLLTRADMED RERFLNARDT 

       130        140        150        160        170        180 
LRALLDNHIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QQGLFTADPR 

       190        200        210        220        230        240 
SNPQAELIKD VYGVDDALRS IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIASGSKPG 

       250        260        270        280        290        300 
VIGDVMEGIS VGTRFHAQAS PLENRKRWIF GAPPAGEITV DEGATAAMLE RGSSLLPKGI 

       310        320        330        340        350        360 
KSVTGNFSRG EVIRICNLQG RDIAHGVSRY NSDALRRIAG HHSQQIDAIL GYEYGPVAVH 


RDDMITR 

« Hide

References

[1]"The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
Nucleic Acids Res. 33:1690-1698(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC-B67.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017220 Genomic DNA. Translation: AAX64228.1.
RefSeqYP_215309.1. NC_006905.1.

3D structure databases

ProteinModelPortalQ57ST3.
SMRQ57ST3. Positions 3-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321314.SC0322.

Proteomic databases

PaxDbQ57ST3.
PRIDEQ57ST3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX64228; AAX64228; SCH_0322.
PATRIC32321122. VBISalEnt136302_0581.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSENT321314:GJCS-335-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_SALCH
AccessionPrimary (citable) accession number: Q57ST3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: May 10, 2005
Last modified: May 14, 2014
This is version 65 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