ID   G6PI_PYRAB              Reviewed;         189 AA.
AC   Q9UXW3; G8ZKS8;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 118.
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; OrderedLocusNames=PYRAB17450; ORFNames=PAB1199;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal-type GPI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCE71219.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248288; CAB50650.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71219.1; ALT_INIT; Genomic_DNA.
DR   PIR; D75026; D75026.
DR   RefSeq; WP_048147196.1; NC_000868.1.
DR   AlphaFoldDB; Q9UXW3; -.
DR   SMR; Q9UXW3; -.
DR   STRING; 272844.PAB1199; -.
DR   GeneID; 1496048; -.
DR   KEGG; pab:PAB1199; -.
DR   PATRIC; fig|272844.11.peg.1864; -.
DR   eggNOG; arCOG02602; Archaea.
DR   HOGENOM; CLU_105797_0_0_2; -.
DR   OrthoDB; 49661at2157; -.
DR   PhylomeDB; Q9UXW3; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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_0000185356"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  21525 MW;  904B3AA0FDDC64F9 CRC64;
     MYKEPLGVKV DFNTGVIPGA KKIVRRLSDM KGYFLDEKSW EELVKKEDPI VYEVYAIEQE
     EKEGDLNFAT TILYPGKVGK EFFFTKGHYH SKKDRAEVYV ALKGKGGMLL QTPEGEARWI
     PMEPGTVVYV PPYWAHRTVN TGDEPFIFLA IYPADAGHDY GTIAERGFSK IVIEENGEVK
     VVDNPRWKS
//