G6PI_ASPOR
ID G6PI_ASPOR Reviewed; 553 AA.
AC Q9HGZ2; Q2TZZ3;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=pgiA; ORFNames=AO090011000659;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.;
RT "Molecular cloning and characterization of glycolytic gene from Aspergillus
RT oryzae.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AB032269; BAB12229.1; -; mRNA.
DR EMBL; AP007171; BAE65122.1; -; Genomic_DNA.
DR RefSeq; XP_001826255.1; XM_001826203.2.
DR AlphaFoldDB; Q9HGZ2; -.
DR SMR; Q9HGZ2; -.
DR STRING; 510516.Q9HGZ2; -.
DR PRIDE; Q9HGZ2; -.
DR EnsemblFungi; BAE65122; BAE65122; AO090011000659.
DR GeneID; 5998358; -.
DR KEGG; aor:AO090011000659; -.
DR VEuPathDB; FungiDB:AO090011000659; -.
DR HOGENOM; CLU_017947_3_0_1; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0005829; C:cytosol; 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 2: Evidence at transcript level;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..553
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180571"
FT ACT_SITE 363
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT ACT_SITE 394
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT ACT_SITE 516
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT BINDING 164..165
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 215..220
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 359
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 363
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 394
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 516
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
SQ SEQUENCE 553 AA; 61214 MW; 06373377B1FF8949 CRC64;
MPAFSQATDL SAWKELQEHH TAVGRNIVLK EAFEKDPQRF EKFSRTFKNT VDNSDILFDF
SKNFLTEETL SLLVKLAKEA NVEELRDAMF KGEHINFTED RAVYHAALRN VSNEPMQVDG
KSVVEDVNSV LEHMKEFSEQ VRSGEWKGYT DKKIDTIINI GIGGSDLGPV MVTEALKPYG
APGMKLHFVS NIDGTHIAEA LKDSNPETTL FLIASKTFTT AETTTNANSA KKWFLETAKD
ESHIAKHFVA LSTNEAEVTK FGIDKKNMFG FESWVGGRYS VWSAIGLSVA LYIGYDNFHQ
FLAGAQAMDK HFREAPLEQN IPAIGGLLSV WYSDFFGAQT HLVAPFDQYL HRFPAYLQQL
SMESNGKAIT RSGEYVKYTT GPILFGEPAT NAQHSFFQLL HQGTKLIPSD FIMAAESHNP
VEGGKHQRML ASNFLAQSEA LMVGKTPEQV KTEGAPDNLV PHKTFLGNRP TTSILAQKIT
PSTLGALIAY YEHLTFTEGA VWNINSFDQW GVELGKVLAK KIQQELETSG AGAGHDASTS
GLLAAFKQKA NLA
