ID   G6PI_MAIZE              Reviewed;         567 AA.
AC   P49105;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=PHI1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B73; TISSUE=Root;
RX   PubMed=7630947; DOI=10.1104/pp.108.3.1295;
RA   Lal S.K., Sachs M.M.;
RT   "Cloning and characterization of an anaerobically induced cDNA encoding
RT   glucose-6-phosphate isomerase from maize.";
RL   Plant Physiol. 108:1295-1296(1995).
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;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U17225; AAA82734.1; -; mRNA.
DR   PIR; T02094; T02094.
DR   RefSeq; NP_001105368.1; NM_001111898.2.
DR   AlphaFoldDB; P49105; -.
DR   SMR; P49105; -.
DR   STRING; 4577.P49105; -.
DR   PaxDb; 4577-GRMZM6G477257_P01; -.
DR   EnsemblPlants; Zm00001eb059230_T001; Zm00001eb059230_P001; Zm00001eb059230.
DR   GeneID; 542313; -.
DR   Gramene; Zm00001eb059230_T001; Zm00001eb059230_P001; Zm00001eb059230.
DR   KEGG; zma:542313; -.
DR   MaizeGDB; 13859; -.
DR   eggNOG; KOG2446; Eukaryota.
DR   InParanoid; P49105; -.
DR   OMA; DWYRQLW; -.
DR   OrthoDB; 1657888at2759; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000007305; Chromosome 1.
DR   ExpressionAtlas; P49105; baseline and differential.
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; 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   2: Evidence at transcript level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..567
FT                   /note="Glucose-6-phosphate isomerase, cytosolic"
FT                   /id="PRO_0000180564"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   567 AA;  62237 MW;  EC135C89DAADACF2 CRC64;
     MASAALICGT EQWKALQAHV GAIQKTHLRD LMADADRCKA MTAEYEGIFL DYSRQQATGE
     TMEKLLKLAD AAKLKEKIEK MFKGEKINST ENRSVLHVAL RAPRDAVINS DGVNVVPEVW
     SVKDKIKQFS ETFRSGSWVG ATGKPLTNVV SVGIGGSFLG PLFVHTALQT DPEAAECAKG
     RQLRFLANVD PVDVARSIKD LDPETTLVVV VSKTFTTAET MLNARTLKEW IVSSLGPQAV
     AKHMIAVSTN LKLVKEFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFPIVQKFLE
     GASSIDNHFY SSSFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQLSME
     SNGKGVSIDG AQLSFETGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GETVSNHDEL MSNFFAQPDA LAYGKTPEQL HSEKVPENLI PHKTFKGNRP SLSLLLPTLS
     AYEVGQLLSI YEHRIAVQGF IWGINSFDQW GVELGKSLAS QVRKQLHGTR MEGKPVEGFN
     HSTSSLLARY LAVKPSTPYD TTVLPKV
//