Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A7B5

- PROB_ECOLI

UniProt

P0A7B5 - PROB_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate 5-kinase

Gene

proB

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.1 PublicationUniRule annotation

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.1 PublicationUniRule annotation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101ATPCurated
Binding sitei50 – 501Substrate
Binding sitei137 – 1371Substrate
Binding sitei149 – 1491Substrate; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1702ATPCurated
Nucleotide bindingi211 – 2177ATPCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate 5-kinase activity Source: EcoCyc
  3. magnesium ion binding Source: EcoCyc
  4. RNA binding Source: InterPro

GO - Biological processi

  1. L-proline biosynthetic process Source: UniProtKB-UniPathway
  2. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10768. proB.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Glutamate 5-kinasePRO_0000109669Add
BLAST

Proteomic databases

PaxDbiP0A7B5.
PRIDEiP0A7B5.

Expressioni

Gene expression databases

GenevestigatoriP0A7B5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP0A7B5. 2 interactions.
STRINGi511145.b0242.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Helixi13 – 164Combined sources
Turni17 – 193Combined sources
Beta strandi20 – 223Combined sources
Helixi25 – 4016Combined sources
Beta strandi44 – 496Combined sources
Helixi52 – 609Combined sources
Helixi69 – 9224Combined sources
Turni93 – 953Combined sources
Beta strandi98 – 1036Combined sources
Helixi105 – 1084Combined sources
Helixi111 – 12616Combined sources
Beta strandi130 – 1356Combined sources
Turni137 – 1393Combined sources
Helixi142 – 1443Combined sources
Helixi149 – 16012Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi175 – 1773Combined sources
Turni179 – 1813Combined sources
Beta strandi190 – 1934Combined sources
Helixi194 – 1963Combined sources
Turni197 – 1993Combined sources
Helixi215 – 22612Combined sources
Beta strandi230 – 2356Combined sources
Helixi241 – 2477Combined sources
Beta strandi252 – 2554Combined sources
Helixi264 – 2707Combined sources
Beta strandi277 – 2804Combined sources
Helixi282 – 29110Combined sources
Helixi297 – 2993Combined sources
Beta strandi300 – 3056Combined sources
Beta strandi312 – 3176Combined sources
Beta strandi322 – 3276Combined sources
Helixi332 – 3387Combined sources
Helixi343 – 3453Combined sources
Helixi346 – 3505Combined sources
Helixi361 – 3633Combined sources
Beta strandi364 – 3663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7B5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini275 – 35379PUAUniRule annotationAdd
BLAST

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

eggNOGiCOG0263.
HOGENOMiHOG000246369.
InParanoidiP0A7B5.
KOiK00931.
OMAiMRMIAGH.
OrthoDBiEOG6PGK7G.
PhylomeDBiP0A7B5.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431E → A(PubMed:6089111)Curated
Sequence conflicti143 – 1431E → A1 PublicationCurated

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.
YP_488537.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73346; AAC73346; b0242.
BAA77911; BAA77911; BAA77911.
GeneIDi12930773.
946425.
KEGGiecj:Y75_p0233.
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 .
PIRi C64749. KIECEG.
RefSeqi NP_414777.1. NC_000913.3.
YP_488537.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P0A7B5.
SMRi P0A7B5. Positions 3-367.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A7B5. 2 interactions.
STRINGi 511145.b0242.

Proteomic databases

PaxDbi P0A7B5.
PRIDEi P0A7B5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73346 ; AAC73346 ; b0242 .
BAA77911 ; BAA77911 ; BAA77911 .
GeneIDi 12930773.
946425.
KEGGi ecj:Y75_p0233.
eco:b0242.
PATRICi 32115599. VBIEscCol129921_0244.

Organism-specific databases

EchoBASEi EB0761.
EcoGenei EG10768. proB.

Phylogenomic databases

eggNOGi COG0263.
HOGENOMi HOG000246369.
InParanoidi P0A7B5.
KOi K00931.
OMAi MRMIAGH.
OrthoDBi EOG6PGK7G.
PhylomeDBi P0A7B5.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .
BioCyci EcoCyc:GLUTKIN-MONOMER.
ECOL316407:JW0232-MONOMER.
MetaCyc:GLUTKIN-MONOMER.
BRENDAi 2.7.2.11. 2026.
SABIO-RK P0A7B5.

Miscellaneous databases

EvolutionaryTracei P0A7B5.
PROi P0A7B5.

Gene expression databases

Genevestigatori P0A7B5.

Family and domain databases

Gene3Di 2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPi MF_00456. ProB.
InterProi IPR001048. 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 ]
Pfami PF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000729. GK. 1 hit.
PRINTSi PR00474. GLU5KINASE.
SMARTi SM00359. PUA. 1 hit.
[Graphical view ]
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR01027. proB. 1 hit.
PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. "Purification and characteristics of a gamma-glutamyl kinase involved in Escherichia coli proline biosynthesis."
    Smith C.J., Deutch A.H., Rushlow K.E.
    J. Bacteriol. 157:545-551(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT.
  8. "Dissection of Escherichia coli glutamate 5-kinase: functional impact of the deletion of the PUA domain."
    Perez-Arellano I., Rubio V., Cervera J.
    FEBS Lett. 579:6903-6908(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT, DOMAIN.
  9. "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.

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 26, 2014
This is version 89 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

External Data

Dasty 3