UniProtKB - P0A7B5 (PROB_ECOLI)
Protein
Glutamate 5-kinase
Gene
proB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.UniRule annotation1 Publication
Catalytic activityi
- EC:2.7.2.11UniRule annotation1 Publication
Activity 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
: L-proline biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.UniRule annotation1 PublicationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- Glutamate 5-kinase (proB), Glutamate 5-kinase (proB)
- Gamma-glutamyl phosphate reductase (proA), Gamma-glutamyl phosphate reductase (proA)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 10 | ATPCurated | 1 | |
Binding sitei | 50 | SubstrateCombined sources1 Publication | 1 | |
Binding sitei | 137 | SubstrateCombined sources1 Publication | 1 | |
Binding sitei | 149 | Substrate; via amide nitrogenCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 169 – 170 | ATPCurated | 2 | |
Nucleotide bindingi | 211 – 217 | ATPCurated | 7 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- glutamate 5-kinase activity Source: EcoCyc
- identical protein binding Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- proline binding Source: EcoCyc
- RNA binding Source: InterPro
GO - Biological processi
- L-proline biosynthetic process Source: EcoCyc
- proline biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Amino-acid biosynthesis, Proline biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:GLUTKIN-MONOMER MetaCyc:GLUTKIN-MONOMER |
BRENDAi | 2.7.2.11, 2026 |
SABIO-RKi | P0A7B5 |
UniPathwayi | UPA00098;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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000109669 | 1 – 367 | Glutamate 5-kinaseAdd BLAST | 367 |
Proteomic databases
jPOSTi | P0A7B5 |
PaxDbi | P0A7B5 |
PRIDEi | P0A7B5 |
Interactioni
Subunit structurei
Homotetramer. Dimer of dimers. May form a complex with gamma-glutamyl phosphate reductase (proA).
3 PublicationsGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4259767, 11 interactors |
IntActi | P0A7B5, 2 interactors |
STRINGi | 511145.b0242 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A7B5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7B5 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 275 – 353 | PUAUniRule annotationAdd BLAST | 79 |
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
Phylogenomic databases
eggNOGi | COG0263, Bacteria |
HOGENOMi | CLU_025400_2_0_6 |
InParanoidi | P0A7B5 |
PhylomeDBi | P0A7B5 |
Family and domain databases
CDDi | cd04242, AAK_G5K_ProB, 1 hit |
Gene3Di | 2.30.130.10, 1 hit 3.40.1160.10, 1 hit |
HAMAPi | MF_00456, ProB, 1 hit |
InterProi | View protein in InterPro IPR036393, AceGlu_kinase-like_sf IPR001048, Asp/Glu/Uridylate_kinase IPR041739, G5K_ProB IPR001057, Glu/AcGlu_kinase IPR011529, Glu_5kinase IPR005715, Glu_5kinase/COase_Synthase IPR019797, Glutamate_5-kinase_CS IPR002478, PUA IPR015947, PUA-like_sf IPR036974, PUA_sf |
Pfami | View protein in Pfam PF00696, AA_kinase, 1 hit PF01472, PUA, 1 hit |
PIRSFi | PIRSF000729, GK, 1 hit |
PRINTSi | PR00474, GLU5KINASE |
SMARTi | View protein in SMART SM00359, PUA, 1 hit |
SUPFAMi | SSF53633, SSF53633, 1 hit SSF88697, SSF88697, 1 hit |
TIGRFAMsi | TIGR01027, proB, 1 hit |
PROSITEi | View protein in PROSITE PS00902, GLUTAMATE_5_KINASE, 1 hit PS50890, PUA, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A7B5-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 143 | E → A (PubMed:6089111).Curated | 1 | |
Sequence conflicti | 143 | E → A (Ref. 2) Curated | 1 |
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 |
PIRi | C64749, KIECEG |
RefSeqi | NP_414777.1, NC_000913.3 WP_001285288.1, NZ_STEB01000020.1 |
Genome annotation databases
EnsemblBacteriai | AAC73346; AAC73346; b0242 BAA77911; BAA77911; BAA77911 |
GeneIDi | 58461056 946425 |
KEGGi | ecj:JW0232 eco:b0242 |
PATRICi | fig|1411691.4.peg.2041 |
Similar proteinsi
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 |
PIRi | C64749, KIECEG |
RefSeqi | NP_414777.1, NC_000913.3 WP_001285288.1, NZ_STEB01000020.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2J5T | X-ray | 2.90 | A/B/C/D/E/F/G/H | 1-367 | [»] | |
2J5V | X-ray | 2.50 | A/B | 1-367 | [»] | |
2W21 | X-ray | 2.95 | A | 1-259 | [»] | |
SMRi | P0A7B5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259767, 11 interactors |
IntActi | P0A7B5, 2 interactors |
STRINGi | 511145.b0242 |
Proteomic databases
jPOSTi | P0A7B5 |
PaxDbi | P0A7B5 |
PRIDEi | P0A7B5 |
Genome annotation databases
EnsemblBacteriai | AAC73346; AAC73346; b0242 BAA77911; BAA77911; BAA77911 |
GeneIDi | 58461056 946425 |
KEGGi | ecj:JW0232 eco:b0242 |
PATRICi | fig|1411691.4.peg.2041 |
Organism-specific databases
EchoBASEi | EB0761 |
Phylogenomic databases
eggNOGi | COG0263, Bacteria |
HOGENOMi | CLU_025400_2_0_6 |
InParanoidi | P0A7B5 |
PhylomeDBi | P0A7B5 |
Enzyme and pathway databases
UniPathwayi | UPA00098;UER00359 |
BioCyci | EcoCyc:GLUTKIN-MONOMER MetaCyc:GLUTKIN-MONOMER |
BRENDAi | 2.7.2.11, 2026 |
SABIO-RKi | P0A7B5 |
Miscellaneous databases
EvolutionaryTracei | P0A7B5 |
PROi | PR:P0A7B5 |
Family and domain databases
CDDi | cd04242, AAK_G5K_ProB, 1 hit |
Gene3Di | 2.30.130.10, 1 hit 3.40.1160.10, 1 hit |
HAMAPi | MF_00456, ProB, 1 hit |
InterProi | View protein in InterPro IPR036393, AceGlu_kinase-like_sf IPR001048, Asp/Glu/Uridylate_kinase IPR041739, G5K_ProB IPR001057, Glu/AcGlu_kinase IPR011529, Glu_5kinase IPR005715, Glu_5kinase/COase_Synthase IPR019797, Glutamate_5-kinase_CS IPR002478, PUA IPR015947, PUA-like_sf IPR036974, PUA_sf |
Pfami | View protein in Pfam PF00696, AA_kinase, 1 hit PF01472, PUA, 1 hit |
PIRSFi | PIRSF000729, GK, 1 hit |
PRINTSi | PR00474, GLU5KINASE |
SMARTi | View protein in SMART SM00359, PUA, 1 hit |
SUPFAMi | SSF53633, SSF53633, 1 hit SSF88697, SSF88697, 1 hit |
TIGRFAMsi | TIGR01027, proB, 1 hit |
PROSITEi | View protein in PROSITE PS00902, GLUTAMATE_5_KINASE, 1 hit PS50890, PUA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PROB_ECOLI | |
Accessioni | P0A7B5Primary (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: | April 7, 2021 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families