ID   G6PI2_CLAXA             Reviewed;         569 AA.
AC   P54242;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic 2;
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=PGIC2;
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; X80667; CAA56694.1; -; Genomic_DNA.
DR   EMBL; X89387; CAA61567.1; -; Genomic_DNA.
DR   PIR; S57831; S57831.
DR   AlphaFoldDB; P54242; -.
DR   SMR; P54242; -.
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 2"
FT                   /id="PRO_0000180562"
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;  62843 MW;  775E889A06D5BEA2 CRC64;
     MATPSLISET EAWKDLKAHL EGIKRTHLRE LMGDTERCQS MMVEFDNIFL DYSRQQASPD
     TINKLYKLAE AAHLKQKIDR MYNGDHINST ENRSVLHVAL RAPRNSAICS DGKNVVPDVW
     NVLDKIKDFS ERVRNGSWVG ATGKELKDVI AVGIGGSFLG PLFVHTALQT DPEASKNARG
     RELRFLANVD PIDAARNISG LNPETTLVVV VSKTFTTAET MLNARTLREW ISSALGVSAV
     AKHMVAVSTN LPLVEKFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFAVVEKFLQ
     GAHSIDQHFS SAPFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQVSME
     SNGKGVSIDG LPLPFESGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GEVVNNHDEL MSNFFAQPDA LAYGKTPEQL KKENVSEHLI PHKTFTGNRP SLSILLPTLD
     AYRIGQLLAI YEHRVAVQGF VWGINSFDQW GVELGKSLAT QVRKQLHASR VKGEPVEEGF
     NFSTKTLLTR YLEATSDVPA DPSTLLPKI