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P0A6T1 (G6PI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:pgi
Ordered Locus Names:b4025, JW3985
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP-Rule MF_00473

Enzyme regulation

Inhibited by sorbitol-6-phosphate (S6P) and activated by CsrA. Ref.6 Ref.8

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_00473

Subunit structure

Homodimer. Ref.11

Subcellular location

Cytoplasm Ref.6.

Induction

Induced by oxidative stress. Ref.6 Ref.8 Ref.10

Disruption phenotype

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. Ref.9 Ref.10

Sequence similarities

Belongs to the GPI family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-909327,EBI-909327

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 549549Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180641

Sites

Active site3551Proton donor By similarity
Active site3861 By similarity
Active site5141 By similarity

Amino acid modifications

Modified residue801N6-acetyllysine Ref.7
Modified residue2281N6-acetyllysine Ref.7
Modified residue2341N6-acetyllysine Ref.7

Experimental info

Sequence conflict3171L → V Ref.1
Sequence conflict3171L → V Ref.2

Secondary structure

.............................................................................................. 549
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6T1 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 74AEDB670A068A01

FASTA54961,530
        10         20         30         40         50         60 
MKNINPTQTA AWQALQKHFD EMKDVTIADL FAKDGDRFSK FSATFDDQML VDYSKNRITE 

        70         80         90        100        110        120 
ETLAKLQDLA KECDLAGAIK SMFSGEKINR TENRAVLHVA LRNRSNTPIL VDGKDVMPEV 

       130        140        150        160        170        180 
NAVLEKMKTF SEAIISGEWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF 

       190        200        210        220        230        240 
VSNVDGTHIA EVLKKVNPET TLFLVASKTF TTQETMTNAH SARDWFLKAA GDEKHVAKHF 

       250        260        270        280        290        300 
AALSTNAKAV GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IVLSIGFDNF VELLSGAHAM 

       310        320        330        340        350        360 
DKHFSTTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ QGNMESNGKY 

       370        380        390        400        410        420 
VDRNGNVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP CDFIAPAITH NPLSDHHQKL 

       430        440        450        460        470        480 
LSNFFAQTEA LAFGKSREVV EQEYRDQGKD PATLDYVVPF KVFEGNRPTN SILLREITPF 

       490        500        510        520        530        540 
SLGALIALYE HKIFTQGVIL NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL 


INRYKAWRG 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15196 Genomic DNA. Translation: CAA33268.1.
U00006 Genomic DNA. Translation: AAC43119.1.
U00096 Genomic DNA. Translation: AAC76995.1.
AP009048 Genomic DNA. Translation: BAE78027.1.
PIRNUEC. H65209.
RefSeqNP_418449.1. NC_000913.3.
YP_492168.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NBUX-ray2.05A/B/C/D/E/F1-549[»]
ProteinModelPortalP0A6T1.
SMRP0A6T1. Positions 1-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35887N.
IntActP0A6T1. 7 interactions.
STRING511145.b4025.

PTM databases

PhosSiteP0810418.

Proteomic databases

PaxDbP0A6T1.
PRIDEP0A6T1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76995; AAC76995; b4025.
BAE78027; BAE78027; BAE78027.
GeneID12932965.
948535.
KEGGecj:Y75_p3912.
eco:b4025.
PATRIC32123579. VBIEscCol129921_4138.

Organism-specific databases

EchoBASEEB0696.
EcoGeneEG10702. pgi.

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261371.
KOK01810.
OMALKMHFVS.
OrthoDBEOG64R61J.
PhylomeDBP0A6T1.
ProtClustDBPRK00179.

Enzyme and pathway databases

BioCycEcoCyc:PGLUCISOM.
ECOL316407:JW3985-MONOMER.
MetaCyc:PGLUCISOM.
SABIO-RKP0A6T1.
UniPathwayUPA00109; UER00181.

Gene expression databases

GenevestigatorP0A6T1.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6T1.
PROP0A6T1.

Entry information

Entry nameG6PI_ECOLI
AccessionPrimary (citable) accession number: P0A6T1
Secondary accession number(s): P11537, Q2M6S9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene