G6PI_ASHGO
ID G6PI_ASHGO Reviewed; 555 AA.
AC Q758L0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glucose-6-phosphate isomerase;
DE Short=GPI;
DE EC=5.3.1.9 {ECO:0000250|UniProtKB:P06744};
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
GN Name=PGI1; OrderedLocusNames=AEL249C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis.
CC {ECO:0000250|UniProtKB:P06744}.
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:0000250|UniProtKB:P06744};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P78917}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52436.1; -; Genomic_DNA.
DR RefSeq; NP_984612.1; NM_209965.1.
DR AlphaFoldDB; Q758L0; -.
DR SMR; Q758L0; -.
DR STRING; 33169.AAS52436; -.
DR EnsemblFungi; AAS52436; AAS52436; AGOS_AEL249C.
DR GeneID; 4620794; -.
DR KEGG; ago:AGOS_AEL249C; -.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; Q758L0; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..555
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180570"
FT ACT_SITE 368
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT ACT_SITE 399
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT ACT_SITE 521
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT BINDING 169..170
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 219..224
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 364
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 368
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 399
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 521
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
SQ SEQUENCE 555 AA; 61257 MW; BE12632073654FDD CRC64;
MATTNTFSDF KLASELPAWA KLQELYEKKG KTLSLKEAFA TDEQRFQKYS RTFSNHDGSK
ILFDFSKNLV DDEILGALAQ LAREANVTQL RDQMFNGEHI NSTEDRAVYH VALRNRANKP
MYVDGKNVAP EVDAVLQHMK EFSEQVRSGA WKGYTGKSIK DVVNIGIGGS DLGPVMVTEA
LKHYAGPLKV HFVSNIDGTH LAETLKEVDP ETTLFLVASK TFTTAETITN ATSAKNWFLS
KTGNNPAHIS KHFAALSTNE TEVAKFGIDT KNMFGFESWV GGRYSVWSAI GLSVALYIGF
DQFEDFLKGA EAVDKHFTST PIEDNIPLLG GLLSVWYNNF FDAQTHLVVP FDQYLHRFPA
YLQQLSMESN GKSVTRGNVF ANYSTGSILF GEPATNAQHS FFQLVHQGTK VIPSDFILAA
QSHNPIENNL HQKMLASNFF AQAEALMVGK DEAQVKAEGA TGGLVPHKVF SGNRPTTSIL
VQKITPANLG ALIAYYEHVT FTEGAIWNIN SFDQWGVELG KVLAKVIGKD LDTTGETTSH
DASTNGLINQ FKAWL
