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A5FQ55 (PROB_DEHMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:DehaBAV1_1093
OrganismDehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1) [Complete proteome] [HAMAP]
Taxonomic identifier216389 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

Protein attributes

Sequence length373 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 – 373373Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081053

Regions

Domain281 – 35979PUA
Nucleotide binding216 – 2227ATP By similarity

Sites

Binding site121ATP By similarity
Binding site521Substrate By similarity
Binding site1391Substrate By similarity
Binding site1541Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FQ55 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 2CA27BF706681DFF

FASTA37340,103
        10         20         30         40         50         60 
MNENCYKRVV IKLGTSLLTG GTGKLDHERM ADLCRQIAEL TRLGTEIVIV SSGAIAAGRS 

        70         80         90        100        110        120 
KMGIRHIPKD VPFKQVLAAI GQSQLMNYYD QLFSPHGLTV AQGLLTKSDL SDRSGYLNAR 

       130        140        150        160        170        180 
NTLLALMELG IITIVNENDV VAIDEIQQAK FGDNDNLSAM VANLIEADLL LILTNIRGLY 

       190        200        210        220        230        240 
TSDPTLHPEA TLITEVKEIT EELEQLAAGS SNKLGTGGMV TKLEAARLAT SSGVTAIIAD 

       250        260        270        280        290        300 
GHIPDIILKL ANGENEGTRF IPSLHKPDSR QRWMMSGLCT RGSICVDDGA AKALRENQKS 

       310        320        330        340        350        360 
LLAAGVQQAE GKFGRGDIVK LTDSHGKRLG YGITNYSSDD ISKIKGLHSQ ELNAVLGGNQ 

       370 
GPEVIHRNNL VVI 

« Hide

References

[1]"Complete sequence of Dehalococcoides sp. BAV1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ritalahti K.M., Loeffler F., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000688 Genomic DNA. Translation: ABQ17673.1.
RefSeqYP_001214551.1. NC_009455.1.

3D structure databases

ProteinModelPortalA5FQ55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216389.DehaBAV1_1093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ17673; ABQ17673; DehaBAV1_1093.
GeneID5131379.
KEGGdeb:DehaBAV1_1093.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycDSP216389:GH6D-1129-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_DEHMB
AccessionPrimary (citable) accession number: A5FQ55
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 48 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