ID G6PI_HELAH Reviewed; 545 AA. AC Q17W92; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 100. 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=Hac_1346; OS Helicobacter acinonychis (strain Sheeba). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=382638; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sheeba; RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120; RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., RA Gressmann H., Achtman M., Schuster S.C.; RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a RT host jump from early humans to large felines."; RL PLoS Genet. 2:1097-1110(2006). 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; AM260522; CAK00084.1; -; Genomic_DNA. DR RefSeq; WP_011578174.1; NC_008229.1. DR AlphaFoldDB; Q17W92; -. DR SMR; Q17W92; -. DR STRING; 382638.Hac_1346; -. DR KEGG; hac:Hac_1346; -. DR eggNOG; COG0166; Bacteria. DR HOGENOM; CLU_017947_3_1_7; -. DR OrthoDB; 140919at2; -. DR BioCyc; HACI382638:HAC_RS05780-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000000775; 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; 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..545 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_1000013975" FT ACT_SITE 351 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 382 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 510 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" SQ SEQUENCE 545 AA; 62423 MW; 5F0F368AB8F795E8 CRC64; MLTQLKTYPK LLKHYEEIKE MHMRDWFSKD KERASRYFVQ FESLSLDYSK NRLNDTTLKL LFELARDCSL KEKIEAMFKG EKINTTEKRA VLHTALRSLN DTEILLDNME VLKSVRSVLK RMRAFSDSVR SGKRLGYTNQ VITDIVNIGI GGSDLGALMV CTALKRYAHP RLKMHFVSNV DGTQILDVLE KLNPASTLFI VASKTFSTQE TLTNALTARK WFVERSGDEK HIAKHFVAVS TNKEAVQQFG IDEHNMFEFW DFVGGRYSLW SAIGLSIMIY LGKKNFNALL KGAYLMDEHF KNAPFESNLP VLMGLIGVWY INFFKSKSHL IAPYDQYLRH FPKFIQQLDM ESNGKRISKK GETIPYDTCP VVWGDMGINA QHAFFQLLHQ GTHLIPIDFI ASLDKKPNAK GHHEILFSNV LAQAQAFMKG KSYEEAFGEL LSKGLEKDEA KDLAHHRVFF GNRPSNILLL EKISPSNMGA LVALYEHKVF VQGVIWDINS FDQWGVELGK ELAVPILQEL EGHKSNAFFD SSTKHLIELY KNYNQ //