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P17856 (PROB_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

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

Enzyme regulation

Proline-mediated feedback inhibition. 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 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
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_0000109723

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

Natural variations

Natural variant1171A → V in proline hyperproducing mutant; 700-X less sensitive to proline inhibition.

Sequences

Sequence LengthMass (Da)Tools
P17856 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 68A2AE8F78353AD5

FASTA36739,170
        10         20         30         40         50         60 
MNGSQTLVVK LGTSVLTGGS LRLNRAHIVE LVRQCAQQHA AGHRIVIVTS GAIAAGREHL 

        70         80         90        100        110        120 
GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ MLLTRADLED RERFLNARDT 

       130        140        150        160        170        180 
MTALLDNRIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QQGLYTADPR 

       190        200        210        220        230        240 
NNPQAELIRE VHGIDDALRA IAGDSVSGLG TGGMGTKLQA ADVACRAGID VVIAAGSKPG 

       250        260        270        280        290        300 
VVADVIEGKP VGTRFHALET PLENRKRWIF GAPPAGEITV DDGAVEAMMA RGSSLLPKGI 

       310        320        330        340        350        360 
REVKGDFSRG EVIRIRNLTG RDLAHGVSRY NSDAMRMIAG HHSQEISEIL GYEYGPVAVH 


RDDMIVS 

« Hide

References

[1]"Analysis of the Serratia marcescens proBA operon and feedback control of proline biosynthesis."
Omori K., Suzuki S., Imai Y., Komatsubara S.
J. Gen. Microbiol. 137:509-517(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sr41.
[2]"Analysis of the mutant proBA operon from a proline-producing strain of Serratia marcescens."
Omori K., Suzuki S., Imai Y., Komatsubara S.
J. Gen. Microbiol. 138:693-699(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTANT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53086 Genomic DNA. Translation: CAA37254.1.
D90351 Genomic DNA. Translation: BAA14364.1.
PIRKISEEM. A49753.

3D structure databases

ProteinModelPortalP17856.
SMRP17856. Positions 4-365.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_SERMA
AccessionPrimary (citable) accession number: P17856
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 19, 2014
This is version 84 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