ID   GPI_THEKO               Reviewed;         189 AA.
AC   Q5JE38;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
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}; OrderedLocusNames=TK1111;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD85300.1; -; Genomic_DNA.
DR   RefSeq; WP_011250062.1; NC_006624.1.
DR   AlphaFoldDB; Q5JE38; -.
DR   SMR; Q5JE38; -.
DR   STRING; 69014.TK1111; -.
DR   EnsemblBacteria; BAD85300; BAD85300; TK1111.
DR   GeneID; 78447624; -.
DR   KEGG; tko:TK1111; -.
DR   PATRIC; fig|69014.16.peg.1087; -.
DR   eggNOG; arCOG02602; Archaea.
DR   HOGENOM; CLU_105797_0_0_2; -.
DR   InParanoid; Q5JE38; -.
DR   OrthoDB; 49661at2157; -.
DR   PhylomeDB; Q5JE38; -.
DR   BRENDA; 5.3.1.9; 5246.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000000536; 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;
KW   Reference proteome.
FT   CHAIN           1..189
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000185359"
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;  21422 MW;  59AC54948A905052 CRC64;
     MEYKRPIGLD IDLETGVIPG AKKLVRRLSD LKGYFLDEEA YNELLKEDPV VYEVYAIEQE
     EKEGDLNFAT TVLYPGKVGK EFFFTKGHFH AKPDRAEIYY GIKGKGGMLL QTPEGEAEWI
     PMGPGTVVYV PPYWAHRTVN TGNEPFIFLA IYPADAGHDY GSIKEKGFSK IVIEEDGEVK
     VVDNPRWKE
//