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G6PI1_CLARO
ID   G6PI1_CLARO             Reviewed;         570 AA.
AC   P54238;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
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 rostrata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX   NCBI_TaxID=49041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Population LDG 8810;
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; X89392; CAA61572.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54238; -.
DR   SMR; P54238; -.
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..570
FT                   /note="Glucose-6-phosphate isomerase, cytosolic 1"
FT                   /id="PRO_0000180557"
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   570 AA;  62875 MW;  262F78005F2CD820 CRC64;
     MASPALISET EAWKDLKAHL EGIKMTHLRE LMGDTERCQS MMVEFDNIFL DYSRQQASPD
     TISKLYKLAD EAHLKQKIDR MYNGDHINTT ENRSVLHVAL RAPRNSAICS DGKNVVPDVW
     SVLDKIKDFS DRVRNGSWIG ATGKELKDVI AVGIGGSFLG PLFVHTALQT DPEASKNARG
     RELRFLANVD PIDVARNISG LNPETTLVVV VSKTFTTAET MLNARTLREW ISSALGPSAV
     AKHMVAVSTN LPLVEKFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFAVVEKFLQ
     GAHSIDQHFS SAPFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQVSME
     SNGKGVSVDG LPLPFESGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GEVVNNHDEL MSNFFAQPDA LAYGKTPEEL KKENVSEHLI PHKTFTGNRP SISILLPTLD
     AYRIGQVLAI YEHRVAVQGF VWGINSFDQW GVELGKSLAT QVRKQLHGSR VKGEPVEEGF
     NFSTKTLLTR YLQATSDVPA DPSTLLPNII
 
 
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