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Reviewed, UniProtKB/Swiss-Prot Q0BIH7 (PROB_BURCM)

Last modified February 9, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Bamb_0487
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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 MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP MF_00456

Subcellular location

Cytoplasm By similarity HAMAP 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 processproline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Glutamate 5-kinase HAMAP MF_00456
PRO_1000081042

Regions

Domain280 – 35879PUA

Sequences

Sequence LengthMass (Da)Tools
Q0BIH7-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: AC8F9240F37766D3

FASTA37239,215
        10         20         30         40         50         60 
MRSIIADSKR LVVKVGSSLV TNDGKGLDHA AIGRWAAQIA ALRAQGKEVV LVSSGAIAEG 

        70         80         90        100        110        120 
MQRLGWSKRP REIDELQAAA AVGQMGLAQV YESRFTEHDI RTAQILLTHA DLADRERYLN 

       130        140        150        160        170        180 
ARSTLLTLLR LGVVPIINEN DTVVTDEIKF GDNDTLGALV ANLIEGDALI ILTDQSGLFT 

       190        200        210        220        230        240 
ADPRKDPNAT LVAEASAGAP DLEAMAGGAG SSLGRGGMLT KILAAKRAAH SGANTVIASG 

       250        260        270        280        290        300 
RETDVLVRLA AGEAIGTQLI ARTARMAARK QWMADHLQVR GHVVIDAGAV EKLTAGGKSL 

       310        320        330        340        350        360 
LPIGVIGVQG AFARGEVIAC VGPDGREVAR GLTNYSSAET KLIHRKPSGE IETVLGYMLE 

       370 
PELIHRDNLV LV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000440 Genomic DNA. Translation: ABI86046.1.
RefSeqYP_772380.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BIH7.

Genome annotation databases

GeneID4308626.
GenomeReviewsGene locus Bamb_0487 in contig CP000440_GR.
KEGGbam:Bamb_0487.
NMPDRfig|339670.3.peg.5782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHBG507643.
OMATDVDRLY.

Family and domain databases

HAMAPMF_00456. ProB.
[Tree]
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu_5kinase.
IPR011529. Glu_5kinase_bact.
IPR019797. Glutamate_5-kinase_CS.
IPR005715. ProB.
IPR002478. PUA.
IPR015947. PUA-like.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_BURCM
AccessionPrimary (citable) accession number: Q0BIH7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents