G6PI_ARALP
ID G6PI_ARALP Reviewed; 560 AA.
AC Q9FXM4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 lyrata subsp. petraea (Northern rock-cress) (Cardaminopsis
OS petraea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=59691;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Strosanden 1;
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}.
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DR EMBL; AB044969; BAB17656.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9FXM4; -.
DR SMR; Q9FXM4; -.
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 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_0000180551"
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; 61748 MW; 7352158EB28CFC48 CRC64;
MASSTALISD TEAWKDLKGH VEDIKKTHLR DLMTDANRCQ SMMMEFDGLL LDYSRQRAPV
ETMDKLLNLA KAAQLTEKIS RMFNGEHINS TENRSVLHVA LRAPKDAVIK ADGKNVVQEV
WNVLDKIKEF SEKIRSGSWV GATGKPLKDV IAIGIGGSFL GPLFVHTALQ TDPEALESAK
GRQLRFLANI DPVDVARNII GLNPETTLVV VVSKTFTTAE TMLNARTLRE WITAALGASA
VAKHMVAVST NLALVEKFGI DPNNAFAFWD WVGGRYSVCS AVGVLPLSLQ YGFSVVEKFL
KGASSIDQHF QSTPFEKNIP VLLGLLSVWN VSFLGYPARA ILPYSQALEK FAPHIQQVSM
ESNGKGVSID GLPLPFETGE IDFGEPGTNG QHSFYQLIHQ GRVIPCDFIG IVKSQQPVYL
KGEVVSNHDE LMSNFFAQPD ALAYGKTPEQ LQKENVSENL IPHKTFSGNR PSLSLLLPEL
TAYNVGQLLA IYEHRVAVQG FVWGINSFDQ WGVELGKVLA TQVRKQLHSS RTQGTALEGF
NYSTTTLLKR YLETSSEPQM