G6PI_THELI
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 03-AUG-2022, entry version 69.
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 Gene3D; 2.60.120.10; -; 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 Pfam; PF06560; GPI; 1.
DR PIRSF; PIRSF019325; Glucose-6-phosphate_isomerase; 1.
DR SUPFAM; SSF51182; SSF51182; 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
