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Q47AC9 (PROB_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Daro_3473
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length372 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 – 372372Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230042

Regions

Domain281 – 35878PUA
Nucleotide binding174 – 1752ATP By similarity
Nucleotide binding216 – 2227ATP By similarity

Sites

Binding site151ATP By similarity
Binding site551Substrate By similarity
Binding site1421Substrate By similarity
Binding site1541Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47AC9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 97CB9D1E33A43607

FASTA37239,293
        10         20         30         40         50         60 
MNPTRLANAK RLVVKVGSAL VTNNGTGLDL SAINDWARQI AVLRQQDKEV VLVSSGAIAC 

        70         80         90        100        110        120 
GMQRLGWAKR PKSVHELQAA AAVGQMGLVQ VYEGAFAKHG LHTAQILLTH DDLADRKRYL 

       130        140        150        160        170        180 
NARSTLNTLL ELGVVPIINE NDTVVTDEIK FGDNDTLGAL VANLIEADAL IILTDQQGLY 

       190        200        210        220        230        240 
TADPRKDPSA TLINEATAGD ETLEGMAGGA GTRIGTGGMI TKVIAAKRAA RSGAHTAIAS 

       250        260        270        280        290        300 
GRETDPIIRL ANGEPVGTLL VSQTQPLAAR KQWLADHLQL AGRLILDAGA VNALHAGKSL 

       310        320        330        340        350        360 
LPIGVIAAEG EFERGAAVAC ISPDGREIAR GLSNYGSGEA RLIARKTTQE IENTLGYVDE 

       370 
PEIIHRDNLI LS 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ48202.1.
RefSeqYP_286672.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47AC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_3473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ48202; AAZ48202; Daro_3473.
GeneID3567341.
KEGGdar:Daro_3473.
PATRIC21605620. VBIDecAro89105_3453.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDARO159087:GI5B-3548-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_DECAR
AccessionPrimary (citable) accession number: Q47AC9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 61 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