G6PI_NEUCR
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 03-AUG-2022, entry version 108.
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; 5141.EFNCRP00000007100; -.
DR PRIDE; Q7S986; -.
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; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..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
