ID G6PI_FRAT1 Reviewed; 540 AA.
AC Q14GS7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=FTF1315c;
OS Francisella tularensis subsp. tularensis (strain FSC 198).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC 198;
RX PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT "Genome sequencing shows that European isolates of Francisella tularensis
RT subspecies tularensis are almost identical to US laboratory strain Schu
RT S4.";
RL PLoS ONE 2:E352-E352(2007).
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; AM286280; CAL09331.1; -; Genomic_DNA.
DR RefSeq; WP_003022047.1; NC_008245.1.
DR AlphaFoldDB; Q14GS7; -.
DR SMR; Q14GS7; -.
DR KEGG; ftf:FTF1315c; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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 Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..540
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000013965"
FT ACT_SITE 346
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 377
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 505
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 540 AA; 61152 MW; 4D34257EBD77D2FD CRC64;
MLFCDDSKKY LKEQNINLKN EFDKDDKRVE KFSLKHQNIY FDYSKNLIND YILKSLLESA
EKSSLKDKIK QMFNGAKINS TEHRAVLHTA LRDLSSTPLI VDGQDIRQEV TKEKQRVKEL
VEKVVSGRWR GFSGKKITDI VNIGIGGSDL GPKMVVRALQ PYHCTDLKVH FVSNVDADSL
LQALHVVDPE TTLFIIASKS FSTEETLLNS ISAREWLLDH YEDEKAVANH FVAISSKLDK
VKEFGIDLEH CYKMWDWVGG RYSLWSSIGM SIAFAIGYDN FEKLLAGAYS VDKHFKETEF
SKNIPVIMAL LASYYSCTYN SQSQALLPYD ERLCYFVDYL QQADMESNGK SVNIAGETVN
YQTGVVLWGG VGTNGQHAFH QLLHQGNIFI PVDFIAIATS HHNYDNHQQA LLANCFAQSQ
ALMFGQSYDM VYNELLKSGL NETQAKELAA HKVIPGNRPS TTILLDELSP YSLGALIALY
EHKIFVQGVL WDINSYDQWG VELGKKLGKN ILKAMNDDSS DEYQNLDDST RQLIAKVKNK
//
