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P0C1E3 (PROB_CORML) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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
OrganismCorynebacterium melassecola
Taxonomic identifier41643 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

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
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_0000236037

Regions

Domain277 – 35175PUA
Nucleotide binding175 – 1762ATP By similarity
Nucleotide binding215 – 2217ATP By similarity

Sites

Binding site141ATP By similarity
Binding site561Substrate By similarity
Binding site1431Substrate By similarity
Binding site1551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C1E3 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: E7CC949DBBDFC77F

FASTA36938,626
        10         20         30         40         50         60 
MRERISNAKR VVVKIGSSSL TNDEDGHTVD PNRINTIVNA LQARMEAGSD LIVVSSGAVA 

        70         80         90        100        110        120 
AGMAPLGLST RPTELAVKQA AAAVGQVHLM HQWGRSFARY GRPIGQVLLT AADAGKRDRA 

       130        140        150        160        170        180 
RNAQRTIDKL RILGAVPIVN ENDTVATTGV NFGDNDRLAA IVAHLVSADA LVLLSDVDGL 

       190        200        210        220        230        240 
FDKNPTDPTA KFISEVRDGN DLKGVIAGDG GKVGTGGMAS KVSAARLASR SGVPVLLTSA 

       250        260        270        280        290        300 
ANIGPALEDA QVGTVFHPKD NRLSAWKFWA LYAADTAGKI RLDDGAVEAV TSGGKSLLAV 

       310        320        330        340        350        360 
GITEIIGDFQ QGEIVEILGP AGQIIGRGEV SYDSDTLQSM VGMQTQDLPD GMQRPVVHAD 


YLSNYASRA 

« Hide

References

[1]"Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: a natural bypass of the proA step."
Ankri S., Serebrijski I., Reyes O., Leblon G.
J. Bacteriol. 178:4412-4419(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 17965 / AS B-4821.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31230 Genomic DNA. Translation: AAC44174.1.
PIRT50666.

3D structure databases

ProteinModelPortalP0C1E3.
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_CORML
AccessionPrimary (citable) accession number: P0C1E3
Secondary accession number(s): P46546
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 43 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