ID   G6PI2_CLALE             Reviewed;         569 AA.
AC   P29333;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic 2A;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=PGI3;
DE            Short=PGI;
DE   AltName: Full=Phosphoglucose isomerase;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=PGIC2-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=1643281; DOI=10.1007/bf00027071;
RA   Thomas B.R., Laudencia-Chingcuanco D.L., Gottlieb L.D.;
RT   "Molecular analysis of the plant gene encoding cytosolic phosphoglucose
RT   isomerase.";
RL   Plant Mol. Biol. 19:745-757(1992).
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; X64332; CAA45616.1; -; Genomic_DNA.
DR   EMBL; X89385; CAA61565.1; -; Genomic_DNA.
DR   PIR; S23542; S23542.
DR   AlphaFoldDB; P29333; -.
DR   SMR; P29333; -.
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 2A"
FT                   /id="PRO_0000180561"
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;  62854 MW;  A76BA3D41557259B CRC64;
     MATPALISET EAWKDLKAHL EGIKRTHLRE LMGDTERCQS MMVEFDNIFL DYSRQQASPD
     TINKLYKLAE AAHLKQKIDR MYNGDHINST ENRSVLHVAL RAPRNSAICS DGKNVVPDVW
     NVLDKIKDFS ERVRNGSWVG ATGKELKDVI AVGIGGSFLG PLFVHTALQT DPEASKNARG
     RELRFLANVD PIDAARNISG LNPETTLVVV VSKTFTTAET MLNARTLREW ISSALGVAAV
     AKHMVAVSTN LPLVEKFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFAVVEKFLQ
     GAHNIDQHFS SAPFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQVSME
     SNGKGVSIDG LPLPFESGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GEVVNNHDEL MSNFFAQPDA LAYGKTPEEL KKENVSEHLI PHKTFTGNRP CLSILLPTLD
     AYRIGQLLAI YEHRVAVQGF VWGINSFDQW GVELGKSLAT QVRKQLHASR VKGEPVEEGF
     NFSTKTLLTR YLQATTDVPA DPSTLLPNI