ID   G6PI_PYRHO              Reviewed;         189 AA.
AC   O59618;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
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=PH1956;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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=BAA31083.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000001; BAA31083.1; ALT_INIT; Genomic_DNA.
DR   PIR; D71211; D71211.
DR   RefSeq; WP_048053524.1; NC_000961.1.
DR   AlphaFoldDB; O59618; -.
DR   SMR; O59618; -.
DR   STRING; 70601.gene:9378969; -.
DR   EnsemblBacteria; BAA31083; BAA31083; BAA31083.
DR   GeneID; 1442804; -.
DR   KEGG; pho:PH1956; -.
DR   eggNOG; arCOG02602; Archaea.
DR   OrthoDB; 49661at2157; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000000752; 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_0000185358"
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;  21596 MW;  D7424F200F378C4F CRC64;
     MYKEPLGVKV DFESGVIEGA KKLVRRLSDM KGYFLDEETW RELVEREDPV VYEVYAVEQE
     EKEGDLNFAT TVLYPGKVGK EFFFTKGHFH AKRDRAEVYI ALKGKGGMLL QTPEGEARWI
     PMEPGTVVYV PPYWAHRTVN TGDEPFIFLA IYPADAGHDY GTIAEKGFSK IVIEENGEVK
     VVDNPRWKN
//