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P0A7B5

- PROB_ECOLI

UniProt

P0A7B5 - PROB_ECOLI

Protein

Glutamate 5-kinase

Gene

proB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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

    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-SubCell

    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 – 116
    Helixi13 – 164
    Turni17 – 193
    Beta strandi20 – 223
    Helixi25 – 4016
    Beta strandi44 – 496
    Helixi52 – 609
    Helixi69 – 9224
    Turni93 – 953
    Beta strandi98 – 1036
    Helixi105 – 1084
    Helixi111 – 12616
    Beta strandi130 – 1356
    Turni137 – 1393
    Helixi142 – 1443
    Helixi149 – 16012
    Beta strandi163 – 1697
    Beta strandi175 – 1773
    Turni179 – 1813
    Beta strandi190 – 1934
    Helixi194 – 1963
    Turni197 – 1993
    Helixi215 – 22612
    Beta strandi230 – 2356
    Helixi241 – 2477
    Beta strandi252 – 2554
    Helixi264 – 2707
    Beta strandi277 – 2804
    Helixi282 – 29110
    Helixi297 – 2993
    Beta strandi300 – 3056
    Beta strandi312 – 3176
    Beta strandi322 – 3276
    Helixi332 – 3387
    Helixi343 – 3453
    Helixi346 – 3505
    Helixi361 – 3633
    Beta strandi364 – 3663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS    50
    GAIAAGREHL GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ 100
    MLLTRADMED RERFLNARDT LRALLDNNIV PVINENDAVA TAEIKVGDND 150
    NLSALAAILA GADKLLLLTD QKGLYTADPR SNPQAELIKD VYGIDDALRA 200
    IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG VIGDVMEGIS 250
    VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI 300
    KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL 350
    GYEYGPVAVH RDDMITR 367
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    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: October 1, 2014
    This is version 87 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