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P0A7B5 (PROB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:b0242, JW0232
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-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

Subunit structure

Homotetramer. Dimer of dimers. Ref.7

Subcellular location

Cytoplasm HAMAP-Rule MF_00456.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Contains 1 PUA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109669

Regions

Domain275 – 35379PUA
Nucleotide binding169 – 1702ATP Probable
Nucleotide binding211 – 2177ATP Probable

Sites

Binding site101ATP Probable
Binding site501Substrate
Binding site1371Substrate
Binding site1491Substrate; via amide nitrogen

Experimental info

Sequence conflict1431E → A Ref.1
Sequence conflict1431E → A Ref.2

Secondary structure

..................................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7B5 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 5541040202EBCCE8

FASTA36739,057
        10         20         30         40         50         60 
MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS GAIAAGREHL 

        70         80         90        100        110        120 
GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ MLLTRADMED RERFLNARDT 

       130        140        150        160        170        180 
LRALLDNNIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QKGLYTADPR 

       190        200        210        220        230        240 
SNPQAELIKD VYGIDDALRA IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG 

       250        260        270        280        290        300 
VIGDVMEGIS VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI 

       310        320        330        340        350        360 
KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL GYEYGPVAVH 


RDDMITR 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli proBA locus by DNA and protein sequencing."
Deutch A.H., Rushlow K.E., Smith C.J.
Nucleic Acids Res. 12:6337-6355(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6 AND 8-12.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 143.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12."
Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B.
J. Mol. Biol. 163:513-532(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
Strain: K12.
[7]"A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase."
Marco-Marin C., Gil-Ortiz F., Perez-Arellano I., Cervera J., Fita I., Rubio V.
J. Mol. Biol. 367:1431-1446(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH 5-OXOPROLINE AND D-GAMMA-GLUTAMYL PHOSPHATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00786 Genomic DNA. Translation: CAA25363.1.
U70214 Genomic DNA. Translation: AAB08662.1.
U00096 Genomic DNA. Translation: AAC73346.1.
AP009048 Genomic DNA. Translation: BAA77911.2.
V00316 Genomic DNA. Translation: CAA23604.1.
PIRKIECEG. C64749.
RefSeqNP_414777.1. NC_000913.3.
YP_488537.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J5TX-ray2.90A/B/C/D/E/F/G/H1-367[»]
2J5VX-ray2.50A/B1-367[»]
2W21X-ray2.95A1-259[»]
ProteinModelPortalP0A7B5.
SMRP0A7B5. Positions 3-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A7B5. 2 interactions.
STRING511145.b0242.

Proteomic databases

PaxDbP0A7B5.
PRIDEP0A7B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73346; AAC73346; b0242.
BAA77911; BAA77911; BAA77911.
GeneID12930773.
946425.
KEGGecj:Y75_p0233.
eco:b0242.
PATRIC32115599. VBIEscCol129921_0244.

Organism-specific databases

EchoBASEEB0761.
EcoGeneEG10768. proB.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
PhylomeDBP0A7B5.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycEcoCyc:GLUTKIN-MONOMER.
ECOL316407:JW0232-MONOMER.
MetaCyc:GLUTKIN-MONOMER.
BRENDA2.7.2.11. 2026.
SABIO-RKP0A7B5.
UniPathwayUPA00098; UER00359.

Gene expression databases

GenevestigatorP0A7B5.

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...

Other

EvolutionaryTraceP0A7B5.
PROP0A7B5.

Entry information

Entry namePROB_ECOLI
AccessionPrimary (citable) accession number: P0A7B5
Secondary accession number(s): P07005, P78293
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene