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Database: UniProt
Entry: Q8RW72_9MYRT
LinkDB: Q8RW72_9MYRT
Original site: Q8RW72_9MYRT 
ID   Q8RW72_9MYRT            Unreviewed;       501 AA.
AC   Q8RW72;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   Name=pgiC1 {ECO:0000313|EMBL:CAC86121.1};
OS   Clarkia modesta.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX   NCBI_TaxID=165267 {ECO:0000313|EMBL:CAC86121.1};
RN   [1] {ECO:0000313|EMBL:CAC86121.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LDG-8612-2b {ECO:0000313|EMBL:CAC86121.1};
RX   PubMed=12038528;
RA   Ford V.S., Gottlieb L.D.;
RT   "Single mutations silence PGiC2 genes in two very recent allotetraploid
RT   species of Clarkia.";
RL   Evolution 56:699-707(2002).
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:0000256|ARBA:ARBA00029321,
CC         ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; AJ312367; CAC86121.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RW72; -.
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   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
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; 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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW   ECO:0000256|RuleBase:RU000612};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
FT   NON_TER         501
FT                   /evidence="ECO:0000313|EMBL:CAC86121.1"
SQ   SEQUENCE   501 AA;  55304 MW;  0BCD727224E7F664 CRC64;
     MASPALISET EAWKDLKAHL EDIKMTHLRE LMGDTERCQS MMVEFDNIFL DYSRQQASPD
     TISKLYKLAD AAHLKQKIDR MYNGDHINTT ENRSVLHVAL RAPRNSAICS DGKNVVPDVW
     NVLDKIKDFS DRVRNGSWIG ATGKKLKDVI AVGIGGSFLG PLFVHTALQT DPESSKNARG
     RELRFLANVD PIDVARNISG LNPETTLVVV VSKTFTTAET MLNARTLREW ISSALGPSAV
     AKHMVAVSTN LPLVEKFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFAVVEKFLQ
     GAHSIDQHFS SAPFEKNVPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQVSME
     SNGKGVSIDG LPLPFESGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GEVVNNHDEL MSNFFAQPDA LAYGKTPEQL KKENVSEHLI PHKTFTGNRP SISILLPTLD
     AYRIGQLLAI YEHRVAVQGF V
//
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