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Database: UniProt
Entry: Q7X9X0_ARAHG
LinkDB: Q7X9X0_ARAHG
Original site: Q7X9X0_ARAHG 
ID   Q7X9X0_ARAHG            Unreviewed;       560 AA.
AC   Q7X9X0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 78.
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};
GN   Name=PgiC1 {ECO:0000313|EMBL:BAC77719.1};
OS   Arabidopsis halleri subsp. gemmifera (Arabis gemmifera).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=63677 {ECO:0000313|EMBL:BAC77719.1};
RN   [1] {ECO:0000313|EMBL:BAC77719.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tsugawa {ECO:0000313|EMBL:BAC77719.1};
RX   PubMed=12716977; DOI=10.1093/molbev/msg124;
RA   Kawabe A., Miyashita N.T.;
RT   "DNA polymorphism in active gene and pseudogene of the cytosolic
RT   phosphoglucose isomerase (PgiC) loci in Arabidopsis halleri ssp.
RT   gemmifera.";
RL   Mol. Biol. Evol. 20:1043-1050(2003).
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; AB100285; BAC77719.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X9X0; -.
DR   UniPathway; UPA00109; UER00181.
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; 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}.
SQ   SEQUENCE   560 AA;  61681 MW;  515081D8F0FCC8CB CRC64;
     MASSTASISD TEAWKDLKGH VEDIKKTHLR DLMTDANRCQ SMMMEFDGLL LDYSRQRATV
     ETVDKLLNLA KAAQLTEKIS RMFNGEHINS TENRSVLHVA LRAPKDAVIK ADGKNVVPEV
     WNVLDKIKEF SEKIRSGSWV GATGKPLKDV IAIGIGGSFL GPLFVHTALQ TDPEALESAK
     GRQLRFLANI DPVDVARNIN GLNPETTLVV VVSKTFTTAE TMLNARTLRE WITAALGASA
     VAKHMVAVST NLALVEKFGI DPNNAFAFWD WVGGRYSVCS AVGVLPLSLQ YGFSVVEKFL
     KGASSIDQHF QSTPIEKNIP VLLGLLSVWN VSFLGYPARA ILPYSQALEK FAPHIQQVSM
     ESNGKGVSID GLPLPFETGE IDFGEPGTNG QHSFYQLIHQ GRVIPCDFIG IVKSQQPVYL
     KGEVVSNHDE LMSNFFAQPD ALAYGKTPEQ LQKENVSENL IPHKTFSGNR PSLSLLLPEL
     TAYNVGQLLA IYEHRVAVQG FVWGINSFDQ WGVELGRVLA THVRKQLHSS RTQGTTLEGF
     NYSTTTLLIR YLETSSEPQM
//
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