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Q30XW1 (PROB_DESDG) 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:Dde_2689
OrganismDesulfovibrio desulfuricans (strain G20) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length379 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 – 379379Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230045

Regions

Domain285 – 36278PUA
Nucleotide binding220 – 2267ATP By similarity

Sites

Binding site201ATP By similarity
Binding site591Substrate By similarity
Binding site1461Substrate By similarity
Binding site1581Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30XW1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 7B73DB116255D1CD

FASTA37940,264
        10         20         30         40         50         60 
MDWQTERGQV LDSARRVVIK VGSAVLTSGN GLDVGVVDNL VAQIADLHGR GVDVVLVSSG 

        70         80         90        100        110        120 
AVSAGRAVLR RCCEIKGMPH KQAASAVGQS RLMHYYDEAF GRHGIISAQI LLTKDDLRSR 

       130        140        150        160        170        180 
HRFLNARNTF AALMDWHAVP IVNENDTVAV RELEFGDNDS LASLLLNVVD ADLFINLTSA 

       190        200        210        220        230        240 
GGVYADNPDT NPDARVMECI ENVHGLNLDV MCGGKTAVGS GGMYSKLLAA RRAAQLGVPT 

       250        260        270        280        290        300 
LILPGRKPDA MLRAFAGDEP GTWVRPEKKT VSARKFWLAY HADPTGSVVV DDGAVKALEA 

       310        320        330        340        350        360 
GKSLLPAGII GVEGGFGRGA LVRVTSAAGA VVAVGLSNYP AADLRRIMGH RTAELTAILG 

       370 
DNQYPEAIHR DNMLMDAVV 

« Hide

References

[1]"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20."
Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. expand/collapse author list , Lapidus A.L., Palumbo A.V., Wall J.D.
J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000112 Genomic DNA. Translation: ABB39485.1.
RefSeqYP_389180.1. NC_007519.1.

3D structure databases

ProteinModelPortalQ30XW1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING207559.Dde_2689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB39485; ABB39485; Dde_2689.
GeneID3757712.
KEGGdde:Dde_2689.
PATRIC21744321. VBIDesDes50040_2656.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDALA207559:GH1L-2407-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_DESDG
AccessionPrimary (citable) accession number: Q30XW1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 6, 2005
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