ID G6PI_CUPTR Reviewed; 547 AA. AC B3R508; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 82. 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=RALTA_A1441; OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=977880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / RC R1; RX PubMed=18490699; DOI=10.1101/gr.076448.108; RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., RA Masson-Boivin C.; RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and RT comparative genomics of rhizobia."; RL Genome Res. 18:1472-1483(2008). 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; CU633749; CAQ69390.1; -; Genomic_DNA. DR RefSeq; WP_012352713.1; NC_010528.1. DR AlphaFoldDB; B3R508; -. DR SMR; B3R508; -. DR GeneID; 29763084; -. DR KEGG; cti:RALTA_A1441; -. DR eggNOG; COG0166; Bacteria. DR HOGENOM; CLU_017947_3_1_4; -. DR BioCyc; CTAI977880:RALTA_RS06900-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000001692; Chromosome 1. 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..547 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_1000125713" FT ACT_SITE 356 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 387 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 508 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" SQ SEQUENCE 547 AA; 59932 MW; F70811411318D230 CRC64; MPTDLHAWNA LLRHHDTLRD AQMRDWFDRE GAQRVAQCSL EAAGLYLDYS KNRITPQTMS LLMQLAAEAG VTRRRDAMFA GEHINTTEDR AVLHVALRAP AGAAFKVDGE AVVPAIHQVL ARMRDFSARV RSGAWKGATG ERITDVINIG IGGSDLGPRM VCRALSHLAD ADGHAAPRMH FVSNVDGTDL AETLVRLDPQ RTLVIVCSKT FTTLETMANA RSARAWFVAS GVAEQDLAKH FVAVSTNTEA VREFGIDPAN MFEFWDWIGG RFSLWSSVGL SITLAVGFDA FSDLLAGGHA MDEHFRTAPL ERNMPVILGM LGVWYRNFWN LPTSCMAPYS TSLELFPAFL QQLEMESNGK SVQLDGQRIR THTSPVVWGT AGTNGQHAYF QQIHQGSQVV PVDFVAPLVP PRRLPGHHAK LLANCFAQAE ALMRGRSADE LRASGLKDEV RIAHMVFDGN RPSNTLLMED LTPNVLGALI ALYEHRTFVQ GVVWRINSFD QWGVELGKIL ARPIEAELTG TATGQHDAST AALIARARAV LKAGAAS //