ID G6PI_THELI Reviewed; 190 AA. AC P84140; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Glucose-6-phosphate isomerase; DE Short=GPI; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase; DE Short=PGI; DE AltName: Full=Phosphohexose isomerase; DE Short=PHI; GN Name=pgiA; OS Thermococcus litoralis. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=2265; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, COFACTOR, ACTIVITY RP REGULATION, SUBUNIT, AND MUTAGENESIS OF HIS-89; HIS-91; GLU-98 AND HIS-137. RX PubMed=12560104; DOI=10.1016/s0014-5793(02)03900-5; RA Jeong J.-J., Fushinobu S., Ito S., Jeon B.S., Shoun H., Wakagi T.; RT "Characterization of the cupin-type phosphoglucose isomerase from the RT hyperthermophilic archaeon Thermococcus litoralis."; RL FEBS Lett. 535:200-204(2003). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), COFACTOR, AND SUBUNIT. RA Jeong J.-J., Fushinobu S., Hidaka M., Shoun H., Wakagi T.; RT "Crystal structure of Thermococcus litoralis phosphoglucose isomerase."; RL Submitted (FEB-2004) to the PDB data bank. 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:0000269|PubMed:12560104}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000269|PubMed:12560104, ECO:0000269|Ref.2}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:12560104, CC ECO:0000269|Ref.2}; CC -!- ACTIVITY REGULATION: Inhibited by mannose 6-phosphate, fructose 1- CC phosphate and fructose 1,6-bisphosphate. Its activity is also inhibited CC by Cobalt (II) ions < EDTA < nickel (II) ions < zinc (II) ions << CC cadmium (II) ions < copper (II) ions. Sodium and potassium ions and CC manganese ions show little or no effect on activity. CC {ECO:0000269|PubMed:12560104}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12560104, ECO:0000269|Ref.2}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the archaeal-type 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; AB081724; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; WP_004067944.1; NC_022084.1. DR PDB; 1J3P; X-ray; 2.02 A; A/B=1-190. DR PDB; 1J3Q; X-ray; 1.85 A; A/B=1-190. DR PDB; 1J3R; X-ray; 2.18 A; A/B=1-190. DR PDBsum; 1J3P; -. DR PDBsum; 1J3Q; -. DR PDBsum; 1J3R; -. DR AlphaFoldDB; P84140; -. DR SMR; P84140; -. DR GeneID; 16550542; -. DR OMA; YPADAGH; -. DR BRENDA; 5.3.1.9; 6302. DR SABIO-RK; P84140; -. DR UniPathway; UPA00109; UER00181. DR EvolutionaryTrace; P84140; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB. DR GO; GO:0006094; P:gluconeogenesis; TAS:UniProtKB. DR GO; GO:0006096; P:glycolytic process; TAS:UniProtKB. DR CDD; cd02218; cupin_PGI; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR HAMAP; MF_01410; G6P_isomerase_arch; 1. DR InterPro; IPR016758; G6P_isomerase_archaea/bacteria. DR InterPro; IPR010551; G6P_isomerase_prok. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR35848:SF6; CUPIN 2 CONSERVED BARREL DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR35848; OXALATE-BINDING PROTEIN; 1. DR Pfam; PF06560; GPI; 1. DR PIRSF; PIRSF019325; Glucose-6-phosphate_isomerase; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Iron; Isomerase; KW Metal-binding. FT CHAIN 1..190 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_0000185360" FT BINDING 89 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 91 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 98 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 137 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT MUTAGEN 89 FT /note="H->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:12560104" FT MUTAGEN 91 FT /note="H->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:12560104" FT MUTAGEN 98 FT /note="E->V: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:12560104" FT MUTAGEN 137 FT /note="H->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:12560104" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:1J3Q" FT TURN 13..15 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 22..27 FT /evidence="ECO:0007829|PDB:1J3Q" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:1J3Q" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:1J3Q" FT HELIX 38..47 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 67..74 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 98..105 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 127..131 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 147..154 FT /evidence="ECO:0007829|PDB:1J3Q" FT HELIX 162..167 FT /evidence="ECO:0007829|PDB:1J3Q" FT STRAND 170..183 FT /evidence="ECO:0007829|PDB:1J3Q" SQ SEQUENCE 190 AA; 21720 MW; 0D91C56E61DD7D3F CRC64; MKYKEPFGVK LDFETGIIEN AKKSVRRLSD MKGYFIDEEA WKKMVEEGDP VVYEVYAIEQ EEKEGDLNFA TTVLYPGKVG NEFFMTKGHY HSKIDRAEVY FALKGKGGML LQTPEGEARF IEMEPGTIVY VPPYWAHRTI NTGDKPFIFL ALYPADAGHD YGTIAEKGFS KIVVEENGKV VVKDNPKWRM //