ID   G6PI1_GEOSE             Reviewed;         449 AA.
AC   P13375;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Glucose-6-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi1 {ECO:0000255|HAMAP-Rule:MF_00473}; Synonyms=pgiA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T521;
RX   PubMed=2532320; DOI=10.1093/nar/17.23.10107;
RA   Tao W., Wang L., Shen R., Sheng Z.;
RT   "Complete nucleotide sequences of two phosphoglucoisomerase isozymes from
RT   Bacillus stearothermophilus.";
RL   Nucleic Acids Res. 17:10107-10108(1989).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
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_00473};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00473}.
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_00473}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00473, ECO:0000305}.
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DR   EMBL; X16639; CAA34634.1; -; Genomic_DNA.
DR   PIR; S15936; NUBSSA.
DR   AlphaFoldDB; P13375; -.
DR   SMR; P13375; -.
DR   SABIO-RK; P13375; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
DR   InterPro; IPR035482; SIS_PGI_2.
DR   PANTHER; PTHR11469; PTHR11469; 1.
DR   Pfam; PF00342; PGI; 2.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Phosphoprotein.
FT   CHAIN           1..449
FT                   /note="Glucose-6-phosphate isomerase 1"
FT                   /id="PRO_0000180591"
FT   ACT_SITE        290
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   MOD_RES         38
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   449 AA;  50337 MW;  89C1FA04A393DFDC CRC64;
     MTHIRFDYSK ALSFFGEHEL TYLRDAVKVA HHSLHEKTGV GNDFLGWLDL PVNYDKEEFA
     RIQKAAAKIQ ADSDVLLVIG IGGSYLGARA AIEMLHHSFY NALPKEKRNT PQIIFVGNNI
     SSTYMKEVMD LLEGKDFSIN VISKSGTTTE PAIAFRIFRK LLEEKYGKEE ARKRIYATTD
     RARGALKTLA TAEGYETFII PDDVGGRYSV LTAVGLLPIA VSGANIEEMM KGAAQAREDF
     SSSELEENAA YQYAAIRNIL YNKGKTIELL INYEPALQYF AEWWKQLFGE SEGKDQKGIF
     PASANFSTDL HSLGQYIQEG RRDLFETVLK VEKPRHDLVI EAEENDLDGL NYLAGKTVDF
     VNTKAFEGTL LAHTDGGVPN LVITLPELNE YTFGYLVYFF EKACAMSGYL LGVNPFDQPG
     VEAYKVNMFA LLGKPGYEEK KAELEKRLK