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Q1QA44 (PROB_PSYCK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Pcryo_1682
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length390 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 – 390390Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252990

Regions

Domain295 – 37480PUA
Nucleotide binding188 – 1892ATP By similarity

Sites

Binding site291ATP By similarity
Binding site691Substrate By similarity
Binding site1561Substrate By similarity
Binding site1681Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QA44 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: B55D6445A28F2A16

FASTA39042,687
        10         20         30         40         50         60 
MAVGIENTIE EARFVEQARN FDIQRVIVKI GSSLLTNNGR GLDRTAIYEW AKQIAQLHKQ 

        70         80         90        100        110        120 
GVEVLLVSSG AVAEGVVRMN LEERPKKLAA LQACASVGQM GLIETWWSAL IQYGIQSSQL 

       130        140        150        160        170        180 
LLTHDDLSNR SRYLNTTGAL TQLLEWRVLP VINENDTITI DEIKFGDNDT LGAMAAAMVN 

       190        200        210        220        230        240 
ADLYIILTDQ EGVFTDNPRN NPHARMIRQE RAMADYLFDI AGDGGKLGRG GMLTKIRAGR 

       250        260        270        280        290        300 
LAAMGGCPTV IVSGAIDDVI TRVVSGEAVG TLLTTNDQDK IIARKQWLAA HLRMSGSLIV 

       310        320        330        340        350        360 
DAGAAKAVVE HQKSLLPVGV SEVRGDFDEG DVVEIVHQDT GERIAVGQVN FSSRDACRVA 

       370        380        390 
RERTEQFDRI LGNNEERVVM VHRDNLALTM 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE75459.1.
RefSeqYP_580943.1. NC_007969.1.

3D structure databases

ProteinModelPortalQ1QA44.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335284.Pcryo_1682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE75459; ABE75459; Pcryo_1682.
GeneID4034581.
KEGGpcr:Pcryo_1682.
PATRIC23062933. VBIPsyCry128170_1788.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycPCRY335284:GHE9-1717-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_PSYCK
AccessionPrimary (citable) accession number: Q1QA44
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 60 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