ID   G6PI_NEUCR              Reviewed;         561 AA.
AC   Q7S986;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=pgi-1; Synonyms=emp-2, gpi-1; ORFNames=NCU07281;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002239; EAA32899.1; -; Genomic_DNA.
DR   RefSeq; XP_962135.1; XM_957042.3.
DR   AlphaFoldDB; Q7S986; -.
DR   SMR; Q7S986; -.
DR   STRING; 367110.Q7S986; -.
DR   PaxDb; 5141-EFNCRP00000007100; -.
DR   EnsemblFungi; EAA32899; EAA32899; NCU07281.
DR   GeneID; 3878284; -.
DR   KEGG; ncr:NCU07281; -.
DR   VEuPathDB; FungiDB:NCU07281; -.
DR   HOGENOM; CLU_017947_3_1_1; -.
DR   InParanoid; Q7S986; -.
DR   OMA; DWYRQLW; -.
DR   OrthoDB; 1657888at2759; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; 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   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..561
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180576"
FT   ACT_SITE        370
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   ACT_SITE        525
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   BINDING         171..172
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         222..227
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         366
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         370
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         401
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         525
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
SQ   SEQUENCE   561 AA;  61398 MW;  F21908EC4F38884C CRC64;
     MAPANTLSAW SDLQSHHSKV GKTFVLKDAF KSDPERFSKF ARTFTLPADI SSDSPNATDI
     LFDFSKNLVT EETLDKLVRL AEEAGVEKKR DAMFAGEKIN FTEDRAVYHV ALRNVSNQEM
     KVDGVDVMNT KGGVNEVLQH MKEFSEQVRS GEWKGYTGKK LTNIINIGIG GSDLGPVMVT
     EALKHYGAKD MTLRFVSNVD GTHIAEALAA SDPETTLFLI ASKTFTTAET ITNANTAKSW
     FLEKTGGQGD ITKHFVALST NEAEVTKFGI DAKNMFGFES WVGGRYSVWS AIGLSVALYV
     GYENFHKFLA GAHAMDNHFR TAPLKENIPV LGGILSVWYS NFYNAQTHLI APFDQYLHRF
     PAYLQQLSME SNGKSITSDG SAAKYTTGPI VFGEPCTNAQ HSFFQLVHQG TKLIPADFIL
     AAKSHNPISN NLHQKMLASN YLAQAEALMV GKTAEEVRAE GNVPEHLVPH KVFLGNRPTT
     SILVGGHIGP AELGALIVYY EHLTFTEGAI WDINSFDQWG VELGKVLAKK ILKEIDEPGA
     GSGHDASTGG LLGAFKKYAD F
//