G6PI_ECOLI
ID G6PI_ECOLI Reviewed; 549 AA.
AC P0A6T1; P11537; Q2M6S9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473};
GN OrderedLocusNames=b4025, JW3985;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=2549364; DOI=10.1007/bf00330951;
RA Froman B.E., Tait R.C., Gottlieb L.D.;
RT "Isolation and characterization of the phosphoglucose isomerase gene from
RT Escherichia coli.";
RL Mol. Gen. Genet. 217:126-131(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHYLOGENETIC STUDY.
RC STRAIN=XL1 Blue 2;
RX PubMed=1593646; DOI=10.1007/bf00160467;
RA Smith M.W., Doolittle R.F.;
RT "Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase.";
RL J. Mol. Evol. 34:544-545(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=4344919; DOI=10.1128/jb.112.3.1201-1205.1972;
RA Friedberg I.;
RT "Localization of phosphoglucose isomerase in Escherichia coli and its
RT relation to the induction of the hexose phosphate transport system.";
RL J. Bacteriol. 112:1201-1205(1972).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-228 AND LYS-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=7493933; DOI=10.1074/jbc.270.49.29096;
RA Sabnis N.A., Yang H., Romeo T.;
RT "Pleiotropic regulation of central carbohydrate metabolism in Escherichia
RT coli via the gene csrA.";
RL J. Biol. Chem. 270:29096-29104(1995).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=14511906; DOI=10.1016/s0168-1656(03)00170-6;
RA Kabir M.M., Shimizu K.;
RT "Gene expression patterns for metabolic pathway in pgi knockout Escherichia
RT coli with and without phb genes based on RT-PCR.";
RL J. Biotechnol. 105:11-31(2003).
RN [10]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=18368388; DOI=10.1007/s00203-008-0361-y;
RA Rungrassamee W., Liu X., Pomposiello P.J.;
RT "Activation of glucose transport under oxidative stress in Escherichia
RT coli.";
RL Arch. Microbiol. 190:41-49(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND SUBUNIT.
RX PubMed=22393408; DOI=10.1371/journal.pone.0032498;
RA Totir M., Echols N., Nanao M., Gee C.L., Moskaleva A., Gradia S.,
RA Iavarone A.T., Berger J.M., May A.P., Zubieta C., Alber T.;
RT "Macro-to-micro structural proteomics: native source proteins for high-
RT throughput crystallization.";
RL PLoS ONE 7:E32498-E32498(2012).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00473};
CC -!- ACTIVITY REGULATION: Inhibited by sorbitol-6-phosphate (S6P) and
CC activated by CsrA. {ECO:0000269|PubMed:4344919,
CC ECO:0000269|PubMed:7493933}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22393408}.
CC -!- INTERACTION:
CC P0A6T1; P0A6T1: pgi; NbExp=3; IntAct=EBI-909327, EBI-909327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473,
CC ECO:0000269|PubMed:4344919}.
CC -!- INDUCTION: Induced by oxidative stress. {ECO:0000269|PubMed:18368388}.
CC -!- DISRUPTION PHENOTYPE: One of the main features of pgi mutant is the
CC overproduction of NADPH produced in pentose phosphate (PP) pathway
CC which causes some reducing power imbalance that ultimately affects the
CC cell growth. Cells lacking this gene grow slowly on glucose and utilize
CC glucose primarily via the pentose phosphate pathway as the source of
CC NADPH. They are also hypersensitive to oxidative stress induced by
CC paraquat. {ECO:0000269|PubMed:14511906, ECO:0000269|PubMed:18368388}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15196; CAA33268.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43119.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76995.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78027.1; -; Genomic_DNA.
DR PIR; H65209; NUEC.
DR RefSeq; NP_418449.1; NC_000913.3.
DR RefSeq; WP_000789986.1; NZ_SSZK01000049.1.
DR PDB; 3NBU; X-ray; 2.05 A; A/B/C/D/E/F=1-549.
DR PDBsum; 3NBU; -.
DR AlphaFoldDB; P0A6T1; -.
DR SMR; P0A6T1; -.
DR BioGRID; 4261959; 24.
DR BioGRID; 852829; 1.
DR DIP; DIP-35887N; -.
DR IntAct; P0A6T1; 7.
DR STRING; 511145.b4025; -.
DR iPTMnet; P0A6T1; -.
DR jPOST; P0A6T1; -.
DR PaxDb; P0A6T1; -.
DR PRIDE; P0A6T1; -.
DR EnsemblBacteria; AAC76995; AAC76995; b4025.
DR EnsemblBacteria; BAE78027; BAE78027; BAE78027.
DR GeneID; 948535; -.
DR KEGG; ecj:JW3985; -.
DR KEGG; eco:b4025; -.
DR PATRIC; fig|511145.12.peg.4138; -.
DR EchoBASE; EB0696; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_6; -.
DR InParanoid; P0A6T1; -.
DR OMA; IGVWYIN; -.
DR PhylomeDB; P0A6T1; -.
DR BioCyc; EcoCyc:PGLUCISOM; -.
DR BioCyc; MetaCyc:PGLUCISOM; -.
DR SABIO-RK; P0A6T1; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P0A6T1; -.
DR PRO; PR:P0A6T1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis;
KW Isomerase; Reference proteome.
FT CHAIN 1..549
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180641"
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 386
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 514
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000269|PubMed:18723842"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000269|PubMed:18723842"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000269|PubMed:18723842"
FT CONFLICT 317
FT /note="L -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3NBU"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:3NBU"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 117..135
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 287..306
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3NBU"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 416..433
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:3NBU"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:3NBU"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 479..499
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 511..523
FT /evidence="ECO:0007829|PDB:3NBU"
FT HELIX 535..547
FT /evidence="ECO:0007829|PDB:3NBU"
SQ 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
