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Q6LTX3 (PROB_PHOPR) 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:PBPRA0839
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length378 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 – 378378Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109704

Regions

Domain286 – 36479PUA
Nucleotide binding179 – 1802ATP By similarity
Nucleotide binding221 – 2277ATP By similarity

Sites

Binding site201ATP By similarity
Binding site601Substrate By similarity
Binding site1471Substrate By similarity
Binding site1591Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6LTX3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 81E7943C9C30EDB9

FASTA37840,523
        10         20         30         40         50         60 
MTPPLSDKQT LPPKQTIVVK LGTSVLTGGT LKLDRAHMVE LVRQCAYLRR YGHKVIIVTS 

        70         80         90        100        110        120 
GAIAAGREHL DYPELPKTMA SKQLLAAVGQ SRLIQEWESL FGIYGLHVGQ MLLTRADLDD 

       130        140        150        160        170        180 
RERYLNARDM LIALLDNGII PVVNENDAVA TTEIKVGDND NLSALVGILG GADKLLLLTD 

       190        200        210        220        230        240 
QPGLFTADPR NNPDAELIRE VHTIDETLRK LAGGSAGGLG TGGMATKLQA ADVARRAGIE 

       250        260        270        280        290        300 
VIIAAGSRPD VISDLASGES VGTRFLPLDT PLESRKRWIL AGPPPAGDIV IDAGAAKAVL 

       310        320        330        340        350        360 
ERGSSLLSKG ISEVKGAFER GEVARIFDTN GVLLARGICR YSSRDMAMIV GKHSQEIYKV 

       370 
LGYEYGPVAI HRDDLVVI 

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378665 Genomic DNA. Translation: CAG19252.1.
RefSeqYP_129054.1. NC_006370.1.

3D structure databases

ProteinModelPortalQ6LTX3.
SMRQ6LTX3. Positions 15-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298386.PBPRA0839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG19252; CAG19252; PBPRA0839.
GeneID3123815.
KEGGppr:PBPRA0839.
PATRIC22932399. VBIPhoPro109272_0921.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

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_PHOPR
AccessionPrimary (citable) accession number: Q6LTX3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
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