GPI_THEGJ
ID GPI_THEGJ Reviewed; 189 AA.
AC C5A5R8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=TGAM_1078;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33580.1; -; Genomic_DNA.
DR RefSeq; WP_015858693.1; NC_012804.1.
DR AlphaFoldDB; C5A5R8; -.
DR SMR; C5A5R8; -.
DR STRING; 593117.TGAM_1078; -.
DR PaxDb; C5A5R8; -.
DR EnsemblBacteria; ACS33580; ACS33580; TGAM_1078.
DR GeneID; 7986952; -.
DR KEGG; tga:TGAM_1078; -.
DR PATRIC; fig|593117.10.peg.1077; -.
DR eggNOG; arCOG02602; Archaea.
DR HOGENOM; CLU_105797_0_0_2; -.
DR OMA; YPADAGH; -.
DR OrthoDB; 72912at2157; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000001488; 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 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 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_1000215221"
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; 21433 MW; 1640DB8BE08DA244 CRC64;
MEYKRPFGVK IDLETGVIPG AKRIVRKLSD MRGYFVDEEA YEKLLREDPV VYEVYAIEQE
EREGDLNFAT TVLYPGKVGK EFFFTKGHYH AKADRAEIYY ALKGKGGMLL QTPEGEAEWI
PMEPGTVVYV PPYWAHRTVN TGGEPFVFLA IYPADAGHDY GSIKEKGFSK IVIDEGGEVK
IVDNPRWSV
