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P0A6T1

- G6PI_ECOLI

UniProt

P0A6T1 - G6PI_ECOLI

Protein

Glucose-6-phosphate isomerase

Gene

pgi

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 82 (01 Oct 2014)
      Sequence version 1 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-glucose 6-phosphate = D-fructose 6-phosphate.

    Enzyme regulationi

    Inhibited by sorbitol-6-phosphate (S6P) and activated by CsrA.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei355 – 3551Proton donorBy similarity
    Active sitei386 – 3861By similarity
    Active sitei514 – 5141By similarity

    GO - Molecular functioni

    1. glucose-6-phosphate isomerase activity Source: EcoCyc
    2. identical protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to oxidative stress Source: EcoCyc
    2. gluconeogenesis Source: UniProtKB-HAMAP
    3. glycolytic process Source: EcoCyc

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Gluconeogenesis, Glycolysis

    Enzyme and pathway databases

    BioCyciEcoCyc:PGLUCISOM.
    ECOL316407:JW3985-MONOMER.
    MetaCyc:PGLUCISOM.
    SABIO-RKP0A6T1.
    UniPathwayiUPA00109; UER00181.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucose-6-phosphate isomerase (EC:5.3.1.9)
    Short name:
    GPI
    Alternative name(s):
    Phosphoglucose isomerase
    Short name:
    PGI
    Phosphohexose isomerase
    Short name:
    PHI
    Gene namesi
    Name:pgi
    Ordered Locus Names:b4025, JW3985
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10702. pgi.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    One of the main features of pgi mutant is the overproduction of NADPH produced in pentose phosphate (PP) pathway which causes some reducing power imbalance that ultimately affects the cell growth. Cells lacking this gene grow slowly on glucose and utilize glucose primarily via the pentose phosphate pathway as the source of NADPH. They are also hypersensitive to oxidative stress induced by paraquat.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 549549Glucose-6-phosphate isomerasePRO_0000180641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801N6-acetyllysine1 Publication
    Modified residuei228 – 2281N6-acetyllysine1 Publication
    Modified residuei234 – 2341N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A6T1.
    PRIDEiP0A6T1.

    PTM databases

    PhosSiteiP0810418.

    Expressioni

    Inductioni

    Induced by oxidative stress.1 Publication

    Gene expression databases

    GenevestigatoriP0A6T1.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-909327,EBI-909327

    Protein-protein interaction databases

    DIPiDIP-35887N.
    IntActiP0A6T1. 7 interactions.
    STRINGi511145.b4025.

    Structurei

    Secondary structure

    1
    549
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Helixi10 – 2213
    Helixi27 – 337
    Helixi37 – 404
    Beta strandi41 – 455
    Turni46 – 483
    Beta strandi49 – 524
    Beta strandi55 – 573
    Helixi60 – 7213
    Helixi75 – 839
    Turni90 – 934
    Helixi98 – 1014
    Beta strandi114 – 1163
    Helixi117 – 13519
    Beta strandi149 – 1535
    Helixi156 – 1583
    Helixi160 – 1689
    Helixi170 – 1723
    Beta strandi177 – 1815
    Helixi186 – 1938
    Helixi198 – 2003
    Beta strandi201 – 2066
    Beta strandi208 – 2103
    Helixi213 – 23018
    Helixi233 – 2386
    Beta strandi240 – 2445
    Helixi257 – 2593
    Beta strandi260 – 2623
    Helixi269 – 2713
    Helixi276 – 2783
    Helixi279 – 2857
    Helixi287 – 30620
    Helixi309 – 3113
    Helixi313 – 32614
    Beta strandi332 – 3387
    Helixi340 – 3423
    Helixi345 – 35713
    Beta strandi375 – 3773
    Turni381 – 3844
    Helixi385 – 39410
    Beta strandi395 – 3973
    Beta strandi401 – 4088
    Helixi416 – 43318
    Helixi437 – 44610
    Helixi451 – 4533
    Turni455 – 4573
    Helixi458 – 4614
    Beta strandi469 – 4768
    Helixi479 – 49921
    Helixi508 – 5103
    Helixi511 – 52313
    Helixi535 – 54713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NBUX-ray2.05A/B/C/D/E/F1-549[»]
    ProteinModelPortaliP0A6T1.
    SMRiP0A6T1. Positions 1-549.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6T1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GPI family.Curated

    Phylogenomic databases

    eggNOGiCOG0166.
    HOGENOMiHOG000261371.
    KOiK01810.
    OMAiNCHFVAN.
    OrthoDBiEOG64R61J.
    PhylomeDBiP0A6T1.

    Family and domain databases

    Gene3Di1.10.1390.10. 1 hit.
    HAMAPiMF_00473. G6P_isomerase.
    InterProiIPR001672. G6P_Isomerase.
    IPR023096. G6P_Isomerase_C.
    IPR018189. Phosphoglucose_isomerase_CS.
    [Graphical view]
    PANTHERiPTHR11469. PTHR11469. 1 hit.
    PfamiPF00342. PGI. 1 hit.
    [Graphical view]
    PRINTSiPR00662. G6PISOMERASE.
    PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
    PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
    PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A6T1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNINPTQTA AWQALQKHFD EMKDVTIADL FAKDGDRFSK FSATFDDQML    50
    VDYSKNRITE ETLAKLQDLA KECDLAGAIK SMFSGEKINR TENRAVLHVA 100
    LRNRSNTPIL VDGKDVMPEV NAVLEKMKTF SEAIISGEWK GYTGKAITDV 150
    VNIGIGGSDL GPYMVTEALR PYKNHLNMHF VSNVDGTHIA EVLKKVNPET 200
    TLFLVASKTF TTQETMTNAH SARDWFLKAA GDEKHVAKHF AALSTNAKAV 250
    GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IVLSIGFDNF VELLSGAHAM 300
    DKHFSTTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ 350
    QGNMESNGKY VDRNGNVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP 400
    CDFIAPAITH NPLSDHHQKL LSNFFAQTEA LAFGKSREVV EQEYRDQGKD 450
    PATLDYVVPF KVFEGNRPTN SILLREITPF SLGALIALYE HKIFTQGVIL 500
    NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL INRYKAWRG 549
    Length:549
    Mass (Da):61,530
    Last modified:March 29, 2005 - v1
    Checksum:i74AEDB670A068A01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti317 – 3171L → V(PubMed:2549364)Curated
    Sequence conflicti317 – 3171L → V(PubMed:1593646)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15196 Genomic DNA. Translation: CAA33268.1.
    U00006 Genomic DNA. Translation: AAC43119.1.
    U00096 Genomic DNA. Translation: AAC76995.1.
    AP009048 Genomic DNA. Translation: BAE78027.1.
    PIRiH65209. NUEC.
    RefSeqiNP_418449.1. NC_000913.3.
    YP_492168.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76995; AAC76995; b4025.
    BAE78027; BAE78027; BAE78027.
    GeneIDi12932965.
    948535.
    KEGGiecj:Y75_p3912.
    eco:b4025.
    PATRICi32123579. VBIEscCol129921_4138.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15196 Genomic DNA. Translation: CAA33268.1 .
    U00006 Genomic DNA. Translation: AAC43119.1 .
    U00096 Genomic DNA. Translation: AAC76995.1 .
    AP009048 Genomic DNA. Translation: BAE78027.1 .
    PIRi H65209. NUEC.
    RefSeqi NP_418449.1. NC_000913.3.
    YP_492168.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NBU X-ray 2.05 A/B/C/D/E/F 1-549 [» ]
    ProteinModelPortali P0A6T1.
    SMRi P0A6T1. Positions 1-549.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35887N.
    IntActi P0A6T1. 7 interactions.
    STRINGi 511145.b4025.

    PTM databases

    PhosSitei P0810418.

    Proteomic databases

    PaxDbi P0A6T1.
    PRIDEi P0A6T1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76995 ; AAC76995 ; b4025 .
    BAE78027 ; BAE78027 ; BAE78027 .
    GeneIDi 12932965.
    948535.
    KEGGi ecj:Y75_p3912.
    eco:b4025.
    PATRICi 32123579. VBIEscCol129921_4138.

    Organism-specific databases

    EchoBASEi EB0696.
    EcoGenei EG10702. pgi.

    Phylogenomic databases

    eggNOGi COG0166.
    HOGENOMi HOG000261371.
    KOi K01810.
    OMAi NCHFVAN.
    OrthoDBi EOG64R61J.
    PhylomeDBi P0A6T1.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00181 .
    BioCyci EcoCyc:PGLUCISOM.
    ECOL316407:JW3985-MONOMER.
    MetaCyc:PGLUCISOM.
    SABIO-RK P0A6T1.

    Miscellaneous databases

    EvolutionaryTracei P0A6T1.
    PROi P0A6T1.

    Gene expression databases

    Genevestigatori P0A6T1.

    Family and domain databases

    Gene3Di 1.10.1390.10. 1 hit.
    HAMAPi MF_00473. G6P_isomerase.
    InterProi IPR001672. G6P_Isomerase.
    IPR023096. G6P_Isomerase_C.
    IPR018189. Phosphoglucose_isomerase_CS.
    [Graphical view ]
    PANTHERi PTHR11469. PTHR11469. 1 hit.
    Pfami PF00342. PGI. 1 hit.
    [Graphical view ]
    PRINTSi PR00662. G6PISOMERASE.
    PROSITEi PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
    PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
    PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli."
      Froman B.E., Tait R.C., Gottlieb L.D.
      Mol. Gen. Genet. 217:126-131(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
    2. "Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase."
      Smith M.W., Doolittle R.F.
      J. Mol. Evol. 34:544-545(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHYLOGENETIC STUDY.
      Strain: XL1 Blue 2.
    3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Localization of phosphoglucose isomerase in Escherichia coli and its relation to the induction of the hexose phosphate transport system."
      Friedberg I.
      J. Bacteriol. 112:1201-1205(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION.
    7. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-228 AND LYS-234, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    8. "Pleiotropic regulation of central carbohydrate metabolism in Escherichia coli via the gene csrA."
      Sabnis N.A., Yang H., Romeo T.
      J. Biol. Chem. 270:29096-29104(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "Gene expression patterns for metabolic pathway in pgi knockout Escherichia coli with and without phb genes based on RT-PCR."
      Kabir M.M., Shimizu K.
      J. Biotechnol. 105:11-31(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "Activation of glucose transport under oxidative stress in Escherichia coli."
      Rungrassamee W., Liu X., Pomposiello P.J.
      Arch. Microbiol. 190:41-49(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, INDUCTION.
    11. "Macro-to-micro structural proteomics: native source proteins for high-throughput crystallization."
      Totir M., Echols N., Nanao M., Gee C.L., Moskaleva A., Gradia S., Iavarone A.T., Berger J.M., May A.P., Zubieta C., Alber T.
      PLoS ONE 7:E32498-E32498(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiG6PI_ECOLI
    AccessioniPrimary (citable) accession number: P0A6T1
    Secondary accession number(s): P11537, Q2M6S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 82 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, 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