ID   G6PI1_CLAXA             Reviewed;         568 AA.
AC   P54240;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic 1;
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=PGIC1;
OS   Clarkia xantiana (Gunsight clarkia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX   NCBI_TaxID=3938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND20466557; DOI=10.2307/2419446;
RA   Ford V.S., Thomas B.R., Gottlieb L.D.;
RT   "The same duplication accounts for the PgiC genes in Clarkia xantiana and
RT   C. lewisii (Onagraceae).";
RL   Syst. Bot. 20:147-160(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Population LDG 7436;
RX   AGRICOLA=IND20535960; DOI=10.2307/2419558;
RA   Gottlieb L.D., Ford V.S.;
RT   "Phylogenetic relationships among the sections of Clarkia (Onagraceae)
RT   inferred from the nucleotide sequences of PgiC.";
RL   Syst. Bot. 21:1-18(1996).
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   -!- 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 GPI family. {ECO:0000305}.
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DR   EMBL; X80666; CAA56693.1; -; Genomic_DNA.
DR   EMBL; X89386; CAA61566.1; -; Genomic_DNA.
DR   PIR; S57830; S57830.
DR   AlphaFoldDB; P54240; -.
DR   SMR; P54240; -.
DR   PRIDE; P54240; -.
DR   UniPathway; UPA00109; UER00181.
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-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..568
FT                   /note="Glucose-6-phosphate isomerase, cytosolic 1"
FT                   /id="PRO_0000180559"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   568 AA;  62641 MW;  AD1E3717C799B71C CRC64;
     MASPALISET EAWKDLKAHL EGIKMIHLRE LMGDTERCQS MMVEFDNIFL DYSRQQASPD
     TISKLYKLAD AAHLKQKIDR MYNGDHINST ENRSVLHVAL RAPRNSAICS DGKNVVPDVW
     NVLDKIKDFS DRVRNGSWIG ATGKELKDVI AVGIGGSFLG PLFVHTALQT DPEASKNARG
     RELRFLANVD PIDVARNISG LNPETTLVVV VSKTFTTAET MLNARTLREW ISSALGPSAV
     AKHMVAVSTN LPLVEKFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFAVVEKFLQ
     GAHSIDQHFS SAPFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQVSME
     SNGKGVSIDG LPLPFESGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGI VKSQQPVYLK
     GEVVNNHDEL MSNFFAQPDA LAYGKTPEQL KNENVSEHLI PHKTFTGNRP SISILLPTLD
     AYRIGQLLAI YEHRVAVQGF VWGINSFDQW GVELGKSLAT QVRKQLHASR VKGEPVEGFN
     FSTKTLLTRY LEATSDVPAD PSTLLPNI