ID G6PI_ENCCU Reviewed; 508 AA. AC Q8SRY1; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Probable glucose-6-phosphate isomerase; DE Short=GPI; DE EC=5.3.1.9 {ECO:0000250|UniProtKB:P06744}; DE AltName: Full=Phosphoglucose isomerase; DE Short=PGI; DE AltName: Full=Phosphohexose isomerase; DE Short=PHI; GN OrderedLocusNames=ECU05_0650; OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=284813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., RA Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP DEVELOPMENTAL STAGE. RX PubMed=16691553; DOI=10.1002/pmic.200500796; RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.; RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi RT (microsporidia): a reference map for proteins expressed in late sporogonial RT stages."; RL Proteomics 6:3625-3635(2006). CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6- CC phosphate to fructose-6-phosphate, the second step in glycolysis, and CC the reverse reaction during gluconeogenesis. CC {ECO:0000250|UniProtKB:P06744}. 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:0000250|UniProtKB:P06744}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC {ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06744}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P78917}. CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages. CC {ECO:0000269|PubMed:16691553}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}. 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; AL590445; CAD26584.1; -; Genomic_DNA. DR RefSeq; NP_597407.1; NM_001041273.1. DR AlphaFoldDB; Q8SRY1; -. DR SMR; Q8SRY1; -. DR STRING; 284813.Q8SRY1; -. DR GeneID; 859072; -. DR KEGG; ecu:ECU05_0650; -. DR VEuPathDB; MicrosporidiaDB:ECU05_0650; -. DR HOGENOM; CLU_017947_3_1_1; -. DR InParanoid; Q8SRY1; -. DR OMA; DWYRQLW; -. DR OrthoDB; 1657888at2759; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000819; Chromosome V. DR GO; GO:0005829; C:cytosol; 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-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. 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 1: Evidence at protein level; KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome. FT CHAIN 1..508 FT /note="Probable glucose-6-phosphate isomerase" FT /id="PRO_0000180574" FT ACT_SITE 340 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P06744" FT ACT_SITE 365 FT /evidence="ECO:0000250|UniProtKB:P06744" FT ACT_SITE 474 FT /evidence="ECO:0000250|UniProtKB:P06744" FT BINDING 142..143 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P06745" FT BINDING 193..198 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P06745" FT BINDING 336 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P06745" FT BINDING 340 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P06745" FT BINDING 365 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P06745" FT BINDING 474 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P06745" SQ SEQUENCE 508 AA; 57867 MW; 65376327480E7C8E CRC64; MMRTEIKSLF ENDRDRVKKL TRRASVGDEF IYYDFSKTHL TEEIVDGYLE KMKDFGEKID GMFGGERINF TENRKVLHVA LRDKEVLRMV EGHGDAKLDE DRRMVYDELM KIKAFVEDFD SGRVCGVTGK KLEIVVNIGI GGSDLGPRMV CDALGHYGRR GVETYFISNI DATDTIRVFE KIDPERALFI VVSKTFTTLE TIKNAELAMK LLERKLGRDR SEIASKHFVA VSSNVQEVGK HNISRVFSMW DFVGGRFSLW SAVGMSIALY VGFNNFMRLL KGASAVDEDF RRNRGRSNAE MIHAIAELFY SENGFNNKCI VCYDQYMEKF YLYLQQAEME SNGKQSERGD TGLIVWGGLG TNTQHSFFQL LHQGTRDVLV ELLMPLKPLH EEKEYHNMVV SNCLAQSRGL MVGKKEGSAK ESFRGNRPTI TVCYSKLTPE TLGAMIAHYE HKIFILGLYW GINSFDQPGV TLGKKIATEV LETLECRGDR KYDESTSEIL RLLGCCKK //