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Q24XR7 (PROB_DESHY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:DSY1386
OrganismDesulfitobacterium hafniense (strain Y51) [Complete proteome] [HAMAP]
Taxonomic identifier138119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

Protein attributes

Sequence length369 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 – 369369Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252977

Regions

Domain276 – 34974PUA
Nucleotide binding169 – 1702ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site101ATP By similarity
Binding site501Substrate By similarity
Binding site1371Substrate By similarity
Binding site1491Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q24XR7 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 1F3D25BEF89DF072

FASTA36939,684
        10         20         30         40         50         60 
MSDLRRIVIK VGSSSLNHPE GGLDDQAIQR IAGVIAGIRQ LGVECVLVSS GAVAAGVGKL 

        70         80         90        100        110        120 
GLKTKPKDMA GKQAVAAVGQ GVLIEKYALA LEARGLVCAQ VLLSRLDLAE ASRYRNAQNT 

       130        140        150        160        170        180 
LEQLLRYQVI PIINENDTVA VEELCFGDND RLSALVAGLV HGDLLVILTD VDGLYSANPK 

       190        200        210        220        230        240 
LNPQAELIEE VEDLTQVMHI AGGAGSSMGT GGMVTKLKAA EITTRFGMGM FLLHSKRMEE 

       250        260        270        280        290        300 
IIELIQGERP LGTYFFPAAH RIMGKKRWIA YGGLSEGSIF IDEGAVKALL KGKSLLASGI 

       310        320        330        340        350        360 
TGIDGVWERK ELVRINNPDG IEVARGLVEL SSEELEKVRG KHSEEMLATI PNLEGEEVVH 


RDNMTLMIE 

« Hide

References

[1]"Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195."
Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., Inatomi K., Furukawa K., Inui M., Yukawa H.
J. Bacteriol. 188:2262-2274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008230 Genomic DNA. Translation: BAE83175.1.
RefSeqYP_517619.1. NC_007907.1.

3D structure databases

ProteinModelPortalQ24XR7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING138119.DSY1386.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE83175; BAE83175; DSY1386.
GeneID3954036.
KEGGdsy:DSY1386.
PATRIC21671157. VBIDesHaf65307_1543.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBCLSK2465810.

Enzyme and pathway databases

BioCycDHAF138119:GHT5-1415-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.
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.
PROSITEPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_DESHY
AccessionPrimary (citable) accession number: Q24XR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 57 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