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Q3IEY8 (PROB1_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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 1

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase 1
Short name=GK 1
Gene names
Name:proB1
Ordered Locus Names:PSHAa0279
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length368 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

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 – 368368Glutamate 5-kinase 1 HAMAP-Rule MF_00456
PRO_0000230055

Regions

Domain274 – 34875PUA
Nucleotide binding167 – 1682ATP By similarity
Nucleotide binding209 – 2157ATP By similarity

Sites

Binding site121ATP By similarity
Binding site521Substrate By similarity
Binding site1351Substrate By similarity
Binding site1471Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IEY8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 71D26AC8C04EC235

FASTA36840,037
        10         20         30         40         50         60 
MNKLNWRRIV LKVGSALIAP DQDGCRSRYI LTIAQFIVRC RARGIEVILV SSGSVAAGAH 

        70         80         90        100        110        120 
LFPSDTARSV VMKKAMAAAG QTEMIAMWDR FFDFPSAQLL LTHGDLRDHE RYQSIRETVF 

       130        140        150        160        170        180 
TLLEHGVLPI INENDAVTTD DLKVGDNDNL SAMVAAAADA DALLIFSDVD GLYDKNPNLH 

       190        200        210        220        230        240 
DDAILLPEIK SIDDSIYAMA GCATSAVGTG GMKTKIEAAE KATSHGISTY IINGFKEETF 

       250        260        270        280        290        300 
TRLLAGENPG TIFLPYEKPM QDSVHWMTHT ANEQGEVVVD GSFDKSLEGE TGCIRGDEIM 

       310        320        330        340        350        360 
AVHGEFAIGD TILVRSEDGT RLAKATANYS SCLLSFIADN EQSEFSEKMQ DSIGPVISEK 


HIALLEKS 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TAC 125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI85378.1.
RefSeqYP_338821.1. NC_007481.1.

3D structure databases

ProteinModelPortalQ3IEY8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326442.PSHAa0279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI85378; CAI85378; PSHAa0279.
GeneID3709886.
KEGGpha:PSHAa0279.
PATRIC32294091. VBIPseHal105694_0265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAVISEKHI.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycPHAL326442:GJIU-283-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.
IPR015947. PUA-like_domain.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB1_PSEHT
AccessionPrimary (citable) accession number: Q3IEY8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 62 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