ID   GPI_THEON               Reviewed;         189 AA.
AC   B6YT45;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01410};
DE            Short=GPI {ECO:0000255|HAMAP-Rule:MF_01410};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01410};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_01410};
DE            Short=PGI {ECO:0000255|HAMAP-Rule:MF_01410};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_01410};
DE            Short=PHI {ECO:0000255|HAMAP-Rule:MF_01410};
GN   Name=pgiA {ECO:0000255|HAMAP-Rule:MF_01410};
GN   OrderedLocusNames=TON_0247;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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_01410};
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_01410}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01410}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01410}.
CC   -!- SIMILARITY: Belongs to the archaeal-type GPI family.
CC       {ECO:0000255|HAMAP-Rule:MF_01410}.
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DR   EMBL; CP000855; ACJ15732.1; -; Genomic_DNA.
DR   RefSeq; WP_012571205.1; NC_011529.1.
DR   AlphaFoldDB; B6YT45; -.
DR   SMR; B6YT45; -.
DR   STRING; 523850.TON_0247; -.
DR   GeneID; 7017909; -.
DR   KEGG; ton:TON_0247; -.
DR   PATRIC; fig|523850.10.peg.249; -.
DR   eggNOG; arCOG02602; Archaea.
DR   HOGENOM; CLU_105797_0_0_2; -.
DR   OrthoDB; 49661at2157; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Iron; Isomerase; Metal-binding.
FT   CHAIN           1..189
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_1000145512"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
FT   BINDING         136
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
SQ   SEQUENCE   189 AA;  21253 MW;  B4AE78E487571D65 CRC64;
     MEYKAPIGVK IDLETGVIPG AKKLVRRLSD LKGYFIDEEA YNELLREDPV VYEVYAIEQE
     EKDGDLNFAT TVLYPGKVGK EFFFTKGHYH AKADRAEIYY AIKGKGGMLL QTPEGNAKWV
     PMEPGTVVYV PPYWAHRTVN TGDEPFIFLA IYPADAGHDY GSIKEKGFSK LVIEEGGEVK
     VVDNPKWKA
//