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Reviewed, UniProtKB/Swiss-Prot Q81C10 (PROB_BACCR)

Last modified February 9, 2010. Version 47. 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: BC_2975
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus 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. 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 – 367367Glutamate 5-kinase HAMAP MF_00456
PRO_0000109634

Regions

Domain276 – 35075PUA

Sequences

Sequence LengthMass (Da)Tools
Q81C10-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 36943B09BE683324

FASTA36739,400
        10         20         30         40         50         60 
MKKQRVVVKI GSSSLADSHG GISTEQLSDH VAALARLKED GHEVVLITSG 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 
NADAKKYYFL PEVTEEISSL AGDAGSKLGT GGMKSKIDAA KTALSLGVSV FIGTGRGQEK 

       250        260        270        280        290        300 
FVNVLKGKGD GTYVGNAPQK EMKMNKQWIA LHSLVSGQIE VDAGAATAII QHGKSLLPAG 

       310        320        330        340        350        360 
VTNVSRFFQV GEVVEVVTQQ GRVIGKGQCT YSAEELIDVK GMQSQDIQVR GERHSYEVIH 


RDHWVSL 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP09922.1.
RefSeqNP_832721.1.

3D structure databases

SMRQ81C10. Positions 3-366.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81C10.

Genome annotation databases

GeneID1205323.
GenomeReviewsGene locus BC_2975 in contig AE016877_GR.
KEGGbce:BC2975.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHBG507643.
OMATDVDRLY.

Enzyme and pathway databases

BioCycBCER226900:BC_2975-MONOMER.

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_BACCR
AccessionPrimary (citable) accession number: Q81C10
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: February 9, 2010
This is version 47 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