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Q639W8 (PROB_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:BCE33L2712
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length367 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.

Sequence caution

The sequence AAU17549.1 differs from that shown. Reason: Erroneous initiation.

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 – 367367Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109635

Regions

Domain276 – 35075PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site91ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q639W8 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: CB2765AE4EF2965B

FASTA36739,540
        10         20         30         40         50         60 
MKKQRIVVKI GSSSLADSHE GISKEQLSDH VAALARLKEE GHEVLLITSG AVAAGFSALG 

        70         80         90        100        110        120 
YPSRPVTIKG KQAAAAVGQS LLMQAYTEEF RKYGIVTAQL LLTRSDFSRK EQYSNAYATL 

       130        140        150        160        170        180 
GELLNRSALP IINENDSISL EELTFGDNDM LSALVSGLVS ADMLMIFTDV NGLYDKNPQK 

       190        200        210        220        230        240 
NEDAKKYYFL PEVTEEIASL AGDAGSKLGT GGMKSKVDAA KTALSLGVSV FIGTGRGQEK 

       250        260        270        280        290        300 
FVDVLKGKGD GTYVGNAPQK EMKMNKQWIA LHSVVSGQIE IDAGAATAII QHGKSLLPAG 

       310        320        330        340        350        360 
VTNVSGFFQV GEVVEVMTQQ GRVIGKGQCT YSAEELRDVK GMQSQHIQAR GERHSYEVIH 


RDHWVSL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000001 Genomic DNA. Translation: AAU17549.1. Different initiation.
RefSeqYP_084299.1. NC_006274.1.

3D structure databases

ProteinModelPortalQ639W8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288681.BCZK2712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU17549; AAU17549; BCE33L2712.
GeneID3023397.
KEGGbcz:BCZK2712.
PATRIC18889072. VBIBacCer95304_2874.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
KOK00931.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycBCER288681:GHG7-2780-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_BACCZ
AccessionPrimary (citable) accession number: Q639W8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 70 of the entry and version 2 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