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B4EUV0 (PROB_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:PMI0369
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

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.

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_1000206276

Regions

Domain275 – 35379PUA
Nucleotide binding169 – 1702ATP By similarity
Nucleotide binding211 – 2177ATP By similarity

Sites

Binding site101ATP By similarity
Binding site501Substrate By similarity
Binding site1371Substrate By similarity
Binding site1491Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B4EUV0 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 040C149CB1EA8DD3

FASTA36739,246
        10         20         30         40         50         60 
MSSSQTLVVK LGTSVLTGGS RRLDQSHIVE LVRQCAKQHE KGHRIIIVTS GAIAAGREYL 

        70         80         90        100        110        120 
NYPDLPATIA SKQLLAAVGQ SALIQVWKQL FAIYGIHIGQ MLLTRADIED RERFLNARDT 

       130        140        150        160        170        180 
LHALLDNKII PVINENDAVA TAEIKVGDND NLSALAAILG GADKLLLLTD IEGLYTADPR 

       190        200        210        220        230        240 
SNPDAKLIPE VFDINDELRQ MAGDSVSGLG TGGMATKLQA ATVAGRAGID VVIAAGVKPD 

       250        260        270        280        290        300 
VISKVIDNEP VGTLFHGLKS PLETRKRWIF GAPVAGVIIV DNGAEKAIKE QGSSLLPKGI 

       310        320        330        340        350        360 
KEIKGDFSRG CVIRIQSLQG KDLAHGVAHY NSDALRLIAG HHSQEISQIL GYEYGSVAVH 


RDDMIVS 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR40948.1.
RefSeqYP_002150141.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4EUV0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI0369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR40948; CAR40948; PMI0369.
GeneID6802523.
KEGGpmr:PMI0369.
PATRIC20515385. VBIProMir120933_0352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-365-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_PROMH
AccessionPrimary (citable) accession number: B4EUV0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 45 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