ID   G6PI1_CLALE             Reviewed;         569 AA.
AC   P34796;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic 1A;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=PGI2;
DE            Short=PGI;
DE   AltName: Full=Phosphoglucose isomerase;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=PGIC1-A;
OS   Clarkia lewisii (Farewell-to-spring) (Clarkia bottae).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX   NCBI_TaxID=3936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8293986; DOI=10.1093/genetics/135.3.895;
RA   Thomas B.R., Ford V.S., Pichersky E., Gottlieb L.D.;
RT   "Molecular characterization of duplicate cytosolic phosphoglucose isomerase
RT   genes in Clarkia and comparison to the single gene in Arabidopsis.";
RL   Genetics 135:895-905(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Population LDG 795;
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.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR   EMBL; X71084; CAA50402.1; -; Genomic_DNA.
DR   EMBL; X89384; CAA61564.1; -; Genomic_DNA.
DR   PIR; S41806; S41806.
DR   AlphaFoldDB; P34796; -.
DR   SMR; P34796; -.
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..569
FT                   /note="Glucose-6-phosphate isomerase, cytosolic 1A"
FT                   /id="PRO_0000180555"
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   569 AA;  62689 MW;  67E5E6D34B67BC07 CRC64;
     MASPALISET EAWKDLKAHL EGIKMTHLRE LMGDTERCQS MMVEFDNIFL DYSRQQASPD
     TISKLYKLAD AAHLKQKIDR MYNGDHINTT ENRSVLHVAL RAPRNSAICS DGKNVVPDVW
     NVLDKIKDFS DSVRNGSWIG 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 RVIPCDFIGV VKSQQPVYLK
     GEVVNNHDEL MSNFFAQPDA LAYGKTPEEL KKENVSEHLI PHKTFTGNRP SISILLPTLD
     AYRIGQLLAI YEHRVAVQGF VWGINSFDQW GVELGKSLAT QVRKQLHGSR VKGEPVEEGF
     NFSTKTLLTR YLQATSDVPA DPSTLLPNI