ID   G6PI3_CLALE             Reviewed;         317 AA.
AC   P34797;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic 2B;
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;
DE   Flags: Fragment;
GN   Name=PGIC2-B;
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).
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:0000255|PROSITE-ProRule:PRU00796};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000255|PROSITE-ProRule:PRU00796}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00796}.
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DR   EMBL; X71085; CAA50403.1; -; Genomic_DNA.
DR   PIR; S41807; S41807.
DR   AlphaFoldDB; P34797; -.
DR   SMR; P34797; -.
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; cd05016; SIS_PGI_2; 1.
DR   Gene3D; 1.10.1390.10; -; 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; IPR035482; SIS_PGI_2.
DR   PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SIS domain; 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..317
FT                   /note="Glucose-6-phosphate isomerase, cytosolic 2B"
FT                   /id="PRO_0000180563"
FT   ACT_SITE        108
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00796"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00796"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00796"
FT   NON_TER         1
SQ   SEQUENCE   317 AA;  34993 MW;  2AD10C29083A0C5D CRC64;
     LVEKFGIDPN NAFAFWDWVG GRYSVCSAVG VLPLSLQYGF SVVEKFLQGA HSIDQHFSSA
     PFEKNIPVLL GLLSVWNVSF LGYPARAILP YSQALEKLAP HIQQVSMESN GKGVSIDGLP
     LPFESGEIDF GEPGTNGQHS FYQLIHQGRV IPCDFIGVVK SQQPVYLKGE VVNNHDELMS
     NFFAQPDALA YGKTPAQLKK ENVSEHLIPH KTFTGNRPSL SILLPTLDAY RIGQLLAIYE
     HRVAVQGFVW GINSFDQWGV ELGKSLATQV RKQLHASRVK GEPVEEGFNF STKTLLTRYL
     QATTDVPADP STLLPNI
//