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Protein

Glutamate 5-kinase

Gene

proB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.UniRule annotation1 Publication

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.UniRule annotation1 Publication

Enzyme regulationi

Interaction with gamma-glutamyl phosphate reductase (proA) seems necessary for kinase activity. Requires free Mg2+. Inhibited by proline and ADP.2 Publications

pH dependencei

Optimum pH is 6.5-7.0.1 Publication

Pathwayi: L-proline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate 5-kinase (proB)
  2. Gamma-glutamyl phosphate reductase (proA)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10ATPCurated1
Binding sitei50Substrate1
Binding sitei137Substrate1
Binding sitei149Substrate; via amide nitrogen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 170ATPCurated2
Nucleotide bindingi211 – 217ATPCurated7

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate 5-kinase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • RNA binding Source: InterPro

GO - Biological processi

  • L-proline biosynthetic process Source: UniProtKB-UniPathway
  • proline biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLUTKIN-MONOMER.
ECOL316407:JW0232-MONOMER.
MetaCyc:GLUTKIN-MONOMER.
BRENDAi2.7.2.11. 2026.
SABIO-RKP0A7B5.
UniPathwayiUPA00098; UER00359.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate 5-kinaseUniRule annotation (EC:2.7.2.11UniRule annotation)
Alternative name(s):
Gamma-glutamyl kinaseUniRule annotation
Short name:
GKUniRule annotation
Gene namesi
Name:proBUniRule annotation
Ordered Locus Names:b0242, JW0232
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10768. proB.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001096691 – 367Glutamate 5-kinaseAdd BLAST367

Proteomic databases

EPDiP0A7B5.
PaxDbiP0A7B5.
PRIDEiP0A7B5.

Interactioni

Subunit structurei

Homotetramer. Dimer of dimers. May form a complex with gamma-glutamyl phosphate reductase (proA).3 Publications

Protein-protein interaction databases

BioGridi4259767. 2 interactors.
IntActiP0A7B5. 2 interactors.
STRINGi511145.b0242.

Structurei

Secondary structure

1367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Helixi13 – 16Combined sources4
Turni17 – 19Combined sources3
Beta strandi20 – 22Combined sources3
Helixi25 – 40Combined sources16
Beta strandi44 – 49Combined sources6
Helixi52 – 60Combined sources9
Helixi69 – 92Combined sources24
Turni93 – 95Combined sources3
Beta strandi98 – 103Combined sources6
Helixi105 – 108Combined sources4
Helixi111 – 126Combined sources16
Beta strandi130 – 135Combined sources6
Turni137 – 139Combined sources3
Helixi142 – 144Combined sources3
Helixi149 – 160Combined sources12
Beta strandi163 – 169Combined sources7
Beta strandi175 – 177Combined sources3
Turni179 – 181Combined sources3
Beta strandi190 – 193Combined sources4
Helixi194 – 196Combined sources3
Turni197 – 199Combined sources3
Helixi215 – 226Combined sources12
Beta strandi230 – 235Combined sources6
Helixi241 – 247Combined sources7
Beta strandi252 – 255Combined sources4
Helixi264 – 270Combined sources7
Beta strandi277 – 280Combined sources4
Helixi282 – 291Combined sources10
Helixi297 – 299Combined sources3
Beta strandi300 – 305Combined sources6
Beta strandi312 – 317Combined sources6
Beta strandi322 – 327Combined sources6
Helixi332 – 338Combined sources7
Helixi343 – 345Combined sources3
Helixi346 – 350Combined sources5
Helixi361 – 363Combined sources3
Beta strandi364 – 366Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J5TX-ray2.90A/B/C/D/E/F/G/H1-367[»]
2J5VX-ray2.50A/B1-367[»]
2W21X-ray2.95A1-259[»]
ProteinModelPortaliP0A7B5.
SMRiP0A7B5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7B5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini275 – 353PUAUniRule annotationAdd BLAST79

Domaini

Contains an N-terminal amino acid kinase (AAK) domain and a C-terminal PUA domain. The AAK domain is responsible for catalyzing the reaction and for proline and ADP inhibition. The PUA domain modulates the catalytic and regulatory functions of the AAK domain.1 Publication

Sequence similaritiesi

Belongs to the glutamate 5-kinase family.UniRule annotation
Contains 1 PUA domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CGT. Bacteria.
COG0263. LUCA.
HOGENOMiHOG000246369.
InParanoidiP0A7B5.
KOiK00931.
OMAiVIHRDHW.
PhylomeDBiP0A7B5.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB. 1 hit.
InterProiIPR001048. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF000729. GK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7B5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS
60 70 80 90 100
GAIAAGREHL GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ
110 120 130 140 150
MLLTRADMED RERFLNARDT LRALLDNNIV PVINENDAVA TAEIKVGDND
160 170 180 190 200
NLSALAAILA GADKLLLLTD QKGLYTADPR SNPQAELIKD VYGIDDALRA
210 220 230 240 250
IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG VIGDVMEGIS
260 270 280 290 300
VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI
310 320 330 340 350
KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL
360
GYEYGPVAVH RDDMITR
Length:367
Mass (Da):39,057
Last modified:June 7, 2005 - v1
Checksum:i5541040202EBCCE8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti143E → A (PubMed:6089111).Curated1
Sequence conflicti143E → A (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC64749. KIECEG.
RefSeqiNP_414777.1. NC_000913.3.
WP_001285288.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73346; AAC73346; b0242.
BAA77911; BAA77911; BAA77911.
GeneIDi946425.
KEGGiecj:JW0232.
eco:b0242.
PATRICi32115599. VBIEscCol129921_0244.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC64749. KIECEG.
RefSeqiNP_414777.1. NC_000913.3.
WP_001285288.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J5TX-ray2.90A/B/C/D/E/F/G/H1-367[»]
2J5VX-ray2.50A/B1-367[»]
2W21X-ray2.95A1-259[»]
ProteinModelPortaliP0A7B5.
SMRiP0A7B5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259767. 2 interactors.
IntActiP0A7B5. 2 interactors.
STRINGi511145.b0242.

Proteomic databases

EPDiP0A7B5.
PaxDbiP0A7B5.
PRIDEiP0A7B5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73346; AAC73346; b0242.
BAA77911; BAA77911; BAA77911.
GeneIDi946425.
KEGGiecj:JW0232.
eco:b0242.
PATRICi32115599. VBIEscCol129921_0244.

Organism-specific databases

EchoBASEiEB0761.
EcoGeneiEG10768. proB.

Phylogenomic databases

eggNOGiENOG4105CGT. Bacteria.
COG0263. LUCA.
HOGENOMiHOG000246369.
InParanoidiP0A7B5.
KOiK00931.
OMAiVIHRDHW.
PhylomeDBiP0A7B5.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.
BioCyciEcoCyc:GLUTKIN-MONOMER.
ECOL316407:JW0232-MONOMER.
MetaCyc:GLUTKIN-MONOMER.
BRENDAi2.7.2.11. 2026.
SABIO-RKP0A7B5.

Miscellaneous databases

EvolutionaryTraceiP0A7B5.
PROiP0A7B5.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB. 1 hit.
InterProiIPR001048. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF000729. GK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROB_ECOLI
AccessioniPrimary (citable) accession number: P0A7B5
Secondary accession number(s): P07005, P78293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.