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B9MDZ8 (PROB_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Dtpsy_0773
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length380 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 – 380380Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000193692

Regions

Domain285 – 36379PUA
Nucleotide binding178 – 1792ATP By similarity

Sites

Binding site151ATP By similarity
Binding site591Substrate By similarity
Binding site1461Substrate By similarity
Binding site1581Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B9MDZ8 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 7C1261B962789241

FASTA38040,365
        10         20         30         40         50         60 
MVSSVLRDAR RIVVKVGSSL VTNEGRGLDE VAIGEWCRQL AALVRGQGGE PREVIMVSSG 

        70         80         90        100        110        120 
AIAEGMKRLG WSSRPGEIHE LQAAAAVGQM GLAQMYETKL REQSMGSAQV LLTHADLADR 

       130        140        150        160        170        180 
ERYLNARSTL LTLLRLGVVP VINENDTVVT DEIKFGDNDT LGALVANLVE ADALVILTDQ 

       190        200        210        220        230        240 
KGLYTADPRR DPQAQFVHEA QAGDAALEAM AGGAGSSIGK GGMITKILAA KRAAGSGAST 

       250        260        270        280        290        300 
VIAWGREPDV LLRLARGESI GTLLVAQTQK NQARKQWMVD HLQLRGSVTV DAGAAAKLRE 

       310        320        330        340        350        360 
DGKSLLPIGM VAVEGDFVRG DVIAVRDAGG TEIARGLANY ASAEARLLCR KPSAEFERLL 

       370        380 
GYAAEPEMVH RDNMVVLGAR 

« Hide

References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM32252.1.
RefSeqYP_002552252.1. NC_011992.1.

3D structure databases

ProteinModelPortalB9MDZ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING535289.Dtpsy_0773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM32252; ACM32252; Dtpsy_0773.
GeneID7383713.
KEGGdia:Dtpsy_0773.
PATRIC21778575. VBIDiaSp55748_0800.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAIDGLYSC.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycAEBR535289:GHOO-777-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_ACIET
AccessionPrimary (citable) accession number: B9MDZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 40 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