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Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI)

 G6PI_ECOLI              Reviewed;         549 AA.
P0A6T1; P11537; Q2M6S9;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 1.
28-MAR-2018, entry version 104.
RecName: Full=Glucose-6-phosphate isomerase;
Short=GPI;
EC=5.3.1.9;
AltName: Full=Phosphoglucose isomerase;
Short=PGI;
AltName: Full=Phosphohexose isomerase;
Short=PHI;
Name=pgi; OrderedLocusNames=b4025, JW3985;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
PubMed=2549364; DOI=10.1007/BF00330951;
Froman B.E., Tait R.C., Gottlieb L.D.;
"Isolation and characterization of the phosphoglucose isomerase gene
from Escherichia coli.";
Mol. Gen. Genet. 217:126-131(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHYLOGENETIC STUDY.
STRAIN=XL1 Blue 2;
PubMed=1593646; DOI=10.1007/BF00160467;
Smith M.W., Doolittle R.F.;
"Anomalous phylogeny involving the enzyme glucose-6-phosphate
isomerase.";
J. Mol. Evol. 34:544-545(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8265357; DOI=10.1093/nar/21.23.5408;
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the
region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=4344919;
Friedberg I.;
"Localization of phosphoglucose isomerase in Escherichia coli and its
relation to the induction of the hexose phosphate transport system.";
J. Bacteriol. 112:1201-1205(1972).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-228 AND LYS-234, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[8]
ENZYME REGULATION.
PubMed=7493933; DOI=10.1074/jbc.270.49.29096;
Sabnis N.A., Yang H., Romeo T.;
"Pleiotropic regulation of central carbohydrate metabolism in
Escherichia coli via the gene csrA.";
J. Biol. Chem. 270:29096-29104(1995).
[9]
DISRUPTION PHENOTYPE.
PubMed=14511906; DOI=10.1016/S0168-1656(03)00170-6;
Kabir M.M., Shimizu K.;
"Gene expression patterns for metabolic pathway in pgi knockout
Escherichia coli with and without phb genes based on RT-PCR.";
J. Biotechnol. 105:11-31(2003).
[10]
DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=18368388; DOI=10.1007/s00203-008-0361-y;
Rungrassamee W., Liu X., Pomposiello P.J.;
"Activation of glucose transport under oxidative stress in Escherichia
coli.";
Arch. Microbiol. 190:41-49(2008).
[11]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND SUBUNIT.
PubMed=22393408; DOI=10.1371/journal.pone.0032498;
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.;
"Macro-to-micro structural proteomics: native source proteins for
high-throughput crystallization.";
PLoS ONE 7:E32498-E32498(2012).
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
phosphate.
-!- ENZYME REGULATION: Inhibited by sorbitol-6-phosphate (S6P) and
activated by CsrA. {ECO:0000269|PubMed:4344919,
ECO:0000269|PubMed:7493933}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 2/4.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22393408}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-909327, EBI-909327;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:4344919}.
-!- INDUCTION: Induced by oxidative stress.
{ECO:0000269|PubMed:18368388}.
-!- 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.
{ECO:0000269|PubMed:14511906, ECO:0000269|PubMed:18368388}.
-!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15196; CAA33268.1; -; Genomic_DNA.
EMBL; U00006; AAC43119.1; -; Genomic_DNA.
EMBL; U00096; AAC76995.1; -; Genomic_DNA.
EMBL; AP009048; BAE78027.1; -; Genomic_DNA.
PIR; H65209; NUEC.
RefSeq; NP_418449.1; NC_000913.3.
RefSeq; WP_000789986.1; NZ_LN832404.1.
PDB; 3NBU; X-ray; 2.05 A; A/B/C/D/E/F=1-549.
PDBsum; 3NBU; -.
ProteinModelPortal; P0A6T1; -.
SMR; P0A6T1; -.
BioGrid; 4261959; 24.
DIP; DIP-35887N; -.
IntAct; P0A6T1; 7.
STRING; 316385.ECDH10B_4214; -.
iPTMnet; P0A6T1; -.
EPD; P0A6T1; -.
PaxDb; P0A6T1; -.
PRIDE; P0A6T1; -.
EnsemblBacteria; AAC76995; AAC76995; b4025.
EnsemblBacteria; BAE78027; BAE78027; BAE78027.
GeneID; 948535; -.
KEGG; ecj:JW3985; -.
KEGG; eco:b4025; -.
PATRIC; fig|511145.12.peg.4138; -.
EchoBASE; EB0696; -.
EcoGene; EG10702; pgi.
eggNOG; ENOG4107QP8; Bacteria.
eggNOG; COG0166; LUCA.
HOGENOM; HOG000261371; -.
InParanoid; P0A6T1; -.
KO; K01810; -.
OMA; TNSQHAF; -.
PhylomeDB; P0A6T1; -.
BioCyc; EcoCyc:PGLUCISOM; -.
BioCyc; MetaCyc:PGLUCISOM; -.
SABIO-RK; P0A6T1; -.
UniPathway; UPA00109; UER00181.
EvolutionaryTrace; P0A6T1; -.
PRO; PR:P0A6T1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc.
GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
CDD; cd05015; SIS_PGI_1; 1.
CDD; cd05016; SIS_PGI_2; 1.
Gene3D; 1.10.1390.10; -; 1.
HAMAP; MF_00473; G6P_isomerase; 1.
InterPro; IPR001672; G6P_Isomerase.
InterPro; IPR023096; G6P_Isomerase_C.
InterPro; IPR018189; Phosphoglucose_isomerase_CS.
InterPro; IPR035476; SIS_PGI_1.
InterPro; IPR035482; SIS_PGI_2.
PANTHER; PTHR11469; PTHR11469; 1.
Pfam; PF00342; PGI; 1.
PRINTS; PR00662; G6PISOMERASE.
PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
CHAIN 1 549 Glucose-6-phosphate isomerase.
/FTId=PRO_0000180641.
ACT_SITE 355 355 Proton donor. {ECO:0000250}.
ACT_SITE 386 386 {ECO:0000250}.
ACT_SITE 514 514 {ECO:0000250}.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 228 228 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
CONFLICT 317 317 L -> V (in Ref. 1 and 2). {ECO:0000305}.
HELIX 6 8 {ECO:0000244|PDB:3NBU}.
HELIX 10 22 {ECO:0000244|PDB:3NBU}.
HELIX 27 33 {ECO:0000244|PDB:3NBU}.
HELIX 37 40 {ECO:0000244|PDB:3NBU}.
STRAND 41 45 {ECO:0000244|PDB:3NBU}.
TURN 46 48 {ECO:0000244|PDB:3NBU}.
STRAND 49 52 {ECO:0000244|PDB:3NBU}.
STRAND 55 57 {ECO:0000244|PDB:3NBU}.
HELIX 60 72 {ECO:0000244|PDB:3NBU}.
HELIX 75 83 {ECO:0000244|PDB:3NBU}.
TURN 90 93 {ECO:0000244|PDB:3NBU}.
HELIX 98 101 {ECO:0000244|PDB:3NBU}.
STRAND 114 116 {ECO:0000244|PDB:3NBU}.
HELIX 117 135 {ECO:0000244|PDB:3NBU}.
STRAND 149 153 {ECO:0000244|PDB:3NBU}.
HELIX 156 158 {ECO:0000244|PDB:3NBU}.
HELIX 160 168 {ECO:0000244|PDB:3NBU}.
HELIX 170 172 {ECO:0000244|PDB:3NBU}.
STRAND 177 181 {ECO:0000244|PDB:3NBU}.
HELIX 186 193 {ECO:0000244|PDB:3NBU}.
HELIX 198 200 {ECO:0000244|PDB:3NBU}.
STRAND 201 206 {ECO:0000244|PDB:3NBU}.
STRAND 208 210 {ECO:0000244|PDB:3NBU}.
HELIX 213 230 {ECO:0000244|PDB:3NBU}.
HELIX 233 238 {ECO:0000244|PDB:3NBU}.
STRAND 240 244 {ECO:0000244|PDB:3NBU}.
HELIX 247 250 {ECO:0000244|PDB:3NBU}.
HELIX 257 259 {ECO:0000244|PDB:3NBU}.
STRAND 260 262 {ECO:0000244|PDB:3NBU}.
HELIX 269 271 {ECO:0000244|PDB:3NBU}.
HELIX 276 278 {ECO:0000244|PDB:3NBU}.
HELIX 279 285 {ECO:0000244|PDB:3NBU}.
HELIX 287 306 {ECO:0000244|PDB:3NBU}.
HELIX 309 311 {ECO:0000244|PDB:3NBU}.
HELIX 313 326 {ECO:0000244|PDB:3NBU}.
STRAND 332 338 {ECO:0000244|PDB:3NBU}.
HELIX 340 342 {ECO:0000244|PDB:3NBU}.
HELIX 345 357 {ECO:0000244|PDB:3NBU}.
STRAND 375 377 {ECO:0000244|PDB:3NBU}.
TURN 381 384 {ECO:0000244|PDB:3NBU}.
HELIX 385 394 {ECO:0000244|PDB:3NBU}.
STRAND 395 397 {ECO:0000244|PDB:3NBU}.
STRAND 401 408 {ECO:0000244|PDB:3NBU}.
HELIX 416 433 {ECO:0000244|PDB:3NBU}.
HELIX 437 446 {ECO:0000244|PDB:3NBU}.
HELIX 451 453 {ECO:0000244|PDB:3NBU}.
TURN 455 457 {ECO:0000244|PDB:3NBU}.
HELIX 458 461 {ECO:0000244|PDB:3NBU}.
STRAND 469 476 {ECO:0000244|PDB:3NBU}.
HELIX 479 499 {ECO:0000244|PDB:3NBU}.
HELIX 508 510 {ECO:0000244|PDB:3NBU}.
HELIX 511 523 {ECO:0000244|PDB:3NBU}.
HELIX 535 547 {ECO:0000244|PDB:3NBU}.
SEQUENCE 549 AA; 61530 MW; 74AEDB670A068A01 CRC64;
MKNINPTQTA AWQALQKHFD EMKDVTIADL FAKDGDRFSK FSATFDDQML VDYSKNRITE
ETLAKLQDLA KECDLAGAIK SMFSGEKINR TENRAVLHVA LRNRSNTPIL VDGKDVMPEV
NAVLEKMKTF SEAIISGEWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF
VSNVDGTHIA EVLKKVNPET TLFLVASKTF TTQETMTNAH SARDWFLKAA GDEKHVAKHF
AALSTNAKAV GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IVLSIGFDNF VELLSGAHAM
DKHFSTTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ QGNMESNGKY
VDRNGNVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP CDFIAPAITH NPLSDHHQKL
LSNFFAQTEA LAFGKSREVV EQEYRDQGKD PATLDYVVPF KVFEGNRPTN SILLREITPF
SLGALIALYE HKIFTQGVIL NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL
INRYKAWRG


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