ID   G6PI_AGABI              Reviewed;         551 AA.
AC   Q711G1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Glucose-6-phosphate isomerase;
DE            Short=GPI;
DE            EC=5.3.1.9 {ECO:0000250|UniProtKB:P06744};
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=gpi1;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kingsnorth C.S., Woodhouse C.S., Henderson J., Burton K.S.;
RT   "Characterisation of a senescence locus in Agaricus bisporus.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC       phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC       the reverse reaction during gluconeogenesis.
CC       {ECO:0000250|UniProtKB:P06744}.
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:0000250|UniProtKB:P06744};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06744}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P78917}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR   EMBL; AJ345056; CAC87889.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q711G1; -.
DR   SMR; Q711G1; -.
DR   UniPathway; UPA00109; UER00181.
DR   GO; GO:0005829; C:cytosol; 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-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   Gene3D; 1.10.1390.10; -; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
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; 1.
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.
FT   CHAIN           1..551
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180569"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   BINDING         161..162
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         212..217
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         356
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         360
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         391
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         516
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
SQ   SEQUENCE   551 AA;  61446 MW;  3747B1A074021671 CRC64;
     MTGSLASNYA SWKQLQEIYD KDRAKIVLRD LFAADPQRFS KLSATYNSQS GPGVQILLDY
     SKHLVTEPIL QKLFNLLREA KVEDARDKMF SGEHINTSED RAVLHVALRN FNDFSIKEEG
     VDEVSKVLQH MKEFSESVRS GQWKGYTGKT INTIVNIGIG GSDLGPVMVT EALKPFSKRD
     LNAHFVSNID GTHIAETLRL CDPERTLFIV ASKTFTTQET ITNAESARDW FLGFAKDKAH
     VAKHFVALST NTSAVTAFGI SEANMFQFWD WVGGRYSLWS AIGLSIALVI GFDNFEKLLR
     GAHAMDQHFK TTPLEKNLPA IMAALGIWCN DFYGAQTLAL LPYDQYLHKF ADYFQQGDME
     SNGKFITKNG DRVNYQTGPI IWGASGTNGQ HSFYQLIHQG TKIIPADFMA PATSHNPIAN
     SKHHRILLSN FFAQPEALAF GKTEEEVRKE LGQNASEALV KSKVFEGNRP SSSLMFDKLD
     PATLGALIAL YEHKIFVQGV VWGINSFDQM GVELGKVLAK QILAQLDKSD DVKGHDSSVR
     HLPFILQVDH C