G6PI_ECO7I
ID G6PI_ECO7I Reviewed; 549 AA.
AC B7NRZ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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}; OrderedLocusNames=ECIAI39_4447;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; CU928164; CAR20553.1; -; Genomic_DNA.
DR RefSeq; WP_000789981.1; NC_011750.1.
DR RefSeq; YP_002410320.1; NC_011750.1.
DR AlphaFoldDB; B7NRZ0; -.
DR SMR; B7NRZ0; -.
DR STRING; 585057.ECIAI39_4447; -.
DR EnsemblBacteria; CAR20553; CAR20553; ECIAI39_4447.
DR KEGG; ect:ECIAI39_4447; -.
DR PATRIC; fig|585057.6.peg.4593; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000749; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..549
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125718"
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 MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 549 AA; 61544 MW; D1ACAC157F068F02 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
VDRNGKVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP CDFIAPAITH NPLSDHHQKL
LSNFFAQTEA LAFGKSREVV EQEYRDQGKD PATLDYVVPF KVFEGNRPTN SILLREITPF
SLGALIALYE HKIFTQGVIL NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL
INRYKAWRG
