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Protein

Glucose-6-phosphate isomerase

Gene

pgi

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

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

Pathway: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA), ATP-dependent 6-phosphofructokinase (pfkA)
  4. Fructose-bisphosphate aldolase class 2 (fbaA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

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

GO - Molecular functioni

  • glucose-6-phosphate isomerase activity Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

  • cellular response to oxidative stress Source: EcoCyc
  • gluconeogenesis Source: UniProtKB-HAMAP
  • glycolytic process Source: EcoCyc
Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10702. pgi.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

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.

Expressioni

Inductioni

Induced by oxidative stress.1 Publication

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 – 83Combined sources
Helixi10 – 2213Combined sources
Helixi27 – 337Combined sources
Helixi37 – 404Combined sources
Beta strandi41 – 455Combined sources
Turni46 – 483Combined sources
Beta strandi49 – 524Combined sources
Beta strandi55 – 573Combined sources
Helixi60 – 7213Combined sources
Helixi75 – 839Combined sources
Turni90 – 934Combined sources
Helixi98 – 1014Combined sources
Beta strandi114 – 1163Combined sources
Helixi117 – 13519Combined sources
Beta strandi149 – 1535Combined sources
Helixi156 – 1583Combined sources
Helixi160 – 1689Combined sources
Helixi170 – 1723Combined sources
Beta strandi177 – 1815Combined sources
Helixi186 – 1938Combined sources
Helixi198 – 2003Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi208 – 2103Combined sources
Helixi213 – 23018Combined sources
Helixi233 – 2386Combined sources
Beta strandi240 – 2445Combined sources
Helixi247 – 2504Combined sources
Helixi257 – 2593Combined sources
Beta strandi260 – 2623Combined sources
Helixi269 – 2713Combined sources
Helixi276 – 2783Combined sources
Helixi279 – 2857Combined sources
Helixi287 – 30620Combined sources
Helixi309 – 3113Combined sources
Helixi313 – 32614Combined sources
Beta strandi332 – 3387Combined sources
Helixi340 – 3423Combined sources
Helixi345 – 35713Combined sources
Beta strandi375 – 3773Combined sources
Turni381 – 3844Combined sources
Helixi385 – 39410Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi401 – 4088Combined sources
Helixi416 – 43318Combined sources
Helixi437 – 44610Combined sources
Helixi451 – 4533Combined sources
Turni455 – 4573Combined sources
Helixi458 – 4614Combined sources
Beta strandi469 – 4768Combined sources
Helixi479 – 49921Combined sources
Helixi508 – 5103Combined sources
Helixi511 – 52313Combined sources
Helixi535 – 54713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A6T1.
KOiK01810.
OMAiFELANDC.
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

        10         20         30         40         50
MKNINPTQTA AWQALQKHFD EMKDVTIADL FAKDGDRFSK FSATFDDQML
60 70 80 90 100
VDYSKNRITE ETLAKLQDLA KECDLAGAIK SMFSGEKINR TENRAVLHVA
110 120 130 140 150
LRNRSNTPIL VDGKDVMPEV NAVLEKMKTF SEAIISGEWK GYTGKAITDV
160 170 180 190 200
VNIGIGGSDL GPYMVTEALR PYKNHLNMHF VSNVDGTHIA EVLKKVNPET
210 220 230 240 250
TLFLVASKTF TTQETMTNAH SARDWFLKAA GDEKHVAKHF AALSTNAKAV
260 270 280 290 300
GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IVLSIGFDNF VELLSGAHAM
310 320 330 340 350
DKHFSTTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ
360 370 380 390 400
QGNMESNGKY VDRNGNVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP
410 420 430 440 450
CDFIAPAITH NPLSDHHQKL LSNFFAQTEA LAFGKSREVV EQEYRDQGKD
460 470 480 490 500
PATLDYVVPF KVFEGNRPTN SILLREITPF SLGALIALYE HKIFTQGVIL
510 520 530 540
NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL INRYKAWRG
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:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

EnsemblBacteriaiAAC76995; AAC76995; b4025.
BAE78027; BAE78027; BAE78027.
GeneIDi948535.
KEGGiecj:Y75_p3912.
eco:b4025.
PATRICi32123579. VBIEscCol129921_4138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0A6T1.
PRIDEiP0A6T1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76995; AAC76995; b4025.
BAE78027; BAE78027; BAE78027.
GeneIDi948535.
KEGGiecj:Y75_p3912.
eco:b4025.
PATRICi32123579. VBIEscCol129921_4138.

Organism-specific databases

EchoBASEiEB0696.
EcoGeneiEG10702. pgi.

Phylogenomic databases

eggNOGiCOG0166.
HOGENOMiHOG000261371.
InParanoidiP0A6T1.
KOiK01810.
OMAiFELANDC.
OrthoDBiEOG64R61J.
PhylomeDBiP0A6T1.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6T1.
PROiP0A6T1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 88 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

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 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.