ID   G6PI_ARAHG              Reviewed;         560 AA.
AC   Q9FXM5;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic;
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=PGIC;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Ashibi 56;
RX   PubMed=11063706; DOI=10.1093/genetics/156.3.1339;
RA   Kawabe A., Yamane K., Miyashita N.T.;
RT   "DNA polymorphism at the cytosolic phosphoglucose isomerase (PgiC) locus of
RT   the wild plant Arabidopsis thaliana.";
RL   Genetics 156:1339-1347(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB17655.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB044968; BAB17655.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q9FXM5; -.
DR   SMR; Q9FXM5; -.
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; 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   Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P34795"
FT   CHAIN           2..560
FT                   /note="Glucose-6-phosphate isomerase, cytosolic"
FT                   /id="PRO_0000180549"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P34795"
SQ   SEQUENCE   560 AA;  61754 MW;  3EB74AA686A2172C CRC64;
     MASSTALFCD TEAWKDLKGH VEDIKKTHLR DLMSDANRCQ SMMMEFDGLL LDYSRQRAPV
     ETMDKLLNLA KAAQLTEKIS RMFNGEHINS TENRSVLHVA LRAPKDAVIK ADGKNVVPEV
     WNVLDKIKEF SEKIRSGSWV GATGKPLKDV IAIGIGGSFL GPLFVHTALQ TDPEALESAK
     GRQLRFLANI DPVDVARNIK GLNPETTLVV VVSKTFTTAE TMLNARTLRE WITAALGASA
     VAKHMVAVST NLALVEKFGI DPNNAFAFWD WVGGRYSVCS AVGVLPLSLQ YGFSVVEKFL
     KGASSIDQHF QSTPFEKNIP VLLGLLSVWN VSFLGYPARA ILPYSQALEK FAPHIQQVSM
     ESNGKGVSID GLPLPFETGE VDFGEPGTNG QHSFYQLIHQ GRVIPCDFIG IVKSQQPVYL
     KGEVVSNHDE LMSNFFAQPD ALAYGKTPEQ LQKENVSENL IPHKTFSGNR PSLSLLLPEL
     TAYNVGQLLA IYEHRVAVQG FVWGINSFDQ WGVELGKVLA TQVRKQLHSS RTQGTALEGF
     NYSTTTLLKR YLETSSEPQM
//