ID G6PI_ACET2 Reviewed; 448 AA. AC A3DBX9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 22-FEB-2023, entry version 84. 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=Cthe_0217; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL RC B-4536 / VPI 7372; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 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}. 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; CP000568; ABN51458.1; -; Genomic_DNA. DR RefSeq; WP_003512317.1; NC_009012.1. DR AlphaFoldDB; A3DBX9; -. DR SMR; A3DBX9; -. DR STRING; 203119.Cthe_0217; -. DR EnsemblBacteria; ABN51458; ABN51458; Cthe_0217. DR KEGG; cth:Cthe_0217; -. DR eggNOG; COG0166; Bacteria. DR HOGENOM; CLU_037303_0_1_9; -. DR OMA; CPAYAYG; -. DR OrthoDB; 140919at2; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000002145; 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 HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. 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; Reference proteome. FT CHAIN 1..448 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_1000013960" FT ACT_SITE 290 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 311 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 425 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" SQ SEQUENCE 448 AA; 50287 MW; C2B06430611EFE7F CRC64; MERIKFDYSK ALPFVSEREV AYFENFVRSA HDMLHNKTGA GNDFVGWVDL PVNYDREEFA RIKAAAEKIK SDSDALVVIG IGGSYLGARA AIEMLSHSFH NLMPKSKRNA PEIYFVGNNI SSTYIADLLE VIEGKEISVN VISKSGTTTE PAIAFRIFKE YMENKYGKDG ASKRIYATTD KEKGALRKLA TEEGYETFVV PDDIGGRFSV LTAVGLLPIA VAGIDIDSMM KGAADARELY SNPNLMENDC YKYAAVRNAL YRKNKTIEIM VNYEPSLHYF TEWWKQLYGE SEGKDQKGIF PAGVDFTTDL HSMGQYIQDG LRNIFETVIR VEKPRKNIVI KEEKDNLDGL NFIAGKDVDY VNKKAMEGTV LAHTDGGVPN LVVTVPELSA YYFGNMVYFF EKACGISGYL LGVNPFDQPG VEAYKKNMFA LLGKPGYEEQ RKKLEERL //