G6PI_KLULA
ID G6PI_KLULA Reviewed; 555 AA.
AC P12341; Q6CM26;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
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=RAG2; OrderedLocusNames=KLLA0E23595g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=3419932; DOI=10.1093/nar/16.17.8714;
RA Wesolowski-Louvel M., Goffrini P., Ferrero I.;
RT "The RAG2 gene of the yeast Kluyveromyces lactis codes for a putative
RT phosphoglucose isomerase.";
RL Nucleic Acids Res. 16:8714-8714(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP CHARACTERIZATION.
RX PubMed=1896011; DOI=10.1007/bf00260633;
RA Goffrini P., Wesolowski-Louvel M., Ferrero I.;
RT "A phosphoglucose isomerase gene is involved in the Rag phenotype of the
RT yeast Kluyveromyces lactis.";
RL Mol. Gen. Genet. 228:401-409(1991).
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; X12360; CAA30923.1; -; Genomic_DNA.
DR EMBL; CR382125; CAH00100.1; -; Genomic_DNA.
DR PIR; S01414; NUVKL.
DR RefSeq; XP_455013.1; XM_455013.1.
DR AlphaFoldDB; P12341; -.
DR SMR; P12341; -.
DR STRING; 28985.XP_455013.1; -.
DR EnsemblFungi; CAH00100; CAH00100; KLLA0_E23519g.
DR GeneID; 2894287; -.
DR KEGG; kla:KLLA0_E23519g; -.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; P12341; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; 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 1: Evidence at protein level;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..555
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180575"
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"
FT CONFLICT 233..234
FT /note="SA -> QLEL (in Ref. 1; CAA30923)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="A -> R (in Ref. 1; CAA30923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 61568 MW; F61A9F8806C1E2CB CRC64;
MASKNTYSDF KLATELPAWN QLQSLYEQKG KKLNVKDEFA KDNSRYEKFA KTFVNYDGSK
ILFDFSKNLV DDEILKSLIQ LAKEAKVTSL RDAMFNGEPI NFTEGRAVYH VALRNRSLKP
MYVDGTNVTP EVDAVLQHMK EFTEEVRSGA WKGYTGKSIT DVVNIGIGGS DLGPVMVTEA
LKHYATNLKV HFVSNIDGTH IAETLKDLDH ETTLFLIASK TFTTAETITN ATSAKNWFLS
KNGGDQSHIS KHFAALSTNA TEVEKFGIDT KNMFGFENWV GGRYSVWSAI GLSVALYIGF
DNFEAFLKGA EAVDKHFVET PLEDNIPLLG GLLSVWYNNF FDAQTHLVAP FDQYLHRFPA
YLQQLSMESN GKSVTRGNVF ANYSTGSILF GEPATNAQHS FFQLIHQGTK LIPSDFILAA
QSHNPIENNL HQKMLASNFF AQAEALMVGK DEEQVKSEGA TGGLVPHKVF SGNRPTTSIL
AQKITPATLG ALIAYYEHVT FTEGAIWNIN SFDQWGVELG KVLAKVIGSE LATDNKISSH
DSSTNGLINQ FKEWI
