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G6PI_STAA8
ID   G6PI_STAA8              Reviewed;         443 AA.
AC   Q2FZU0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473};
GN   OrderedLocusNames=SAOUHSC_00900;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
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:0000255|HAMAP-Rule:MF_00473};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00473}.
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DR   EMBL; CP000253; ABD30025.1; -; Genomic_DNA.
DR   RefSeq; WP_000148849.1; NZ_LS483365.1.
DR   RefSeq; YP_499453.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZU0; -.
DR   SMR; Q2FZU0; -.
DR   STRING; 1280.SAXN108_0957; -.
DR   EnsemblBacteria; ABD30025; ABD30025; SAOUHSC_00900.
DR   GeneID; 3921746; -.
DR   KEGG; sao:SAOUHSC_00900; -.
DR   PATRIC; fig|93061.5.peg.821; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_037303_0_1_9; -.
DR   OMA; CPAYAYG; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:Q2FZU0; -.
DR   Proteomes; UP000008816; Chromosome.
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   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
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..443
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000252648"
FT   ACT_SITE        285
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   443 AA;  49822 MW;  AB7C57B429818F4F CRC64;
     MTHIQLDFSK TLEFFGEHEL KQQQEIVKSI HKTIHEGTGA GSDFLGWIDL PVDYDKEEFS
     RIVEASKRIK ENSDVLVVIG IGGSYLGARA AIEMLTSSFR NSNEYPEIVF VGNHLSSTYT
     KELVDYLADK DFSVNVISKS GTTTEPAVAF RLFKQLVEER YGKEEAQKRI FATTDKEKGA
     LKQLATNEGY ETFIVPDDVG GRYSVLTAVG LLPIATAGIN IEAMMIGAAK AREELSSDKL
     EENIAYQYAT IRNILYAKGY TTEMLINYEP SMQYFNEWWK QLFGESEGKD FKGIYPSSAN
     YTTDLHSLGQ YVQEGRRFLF ETVVKVNHPK YDITIEKDSD DLDGLNYLAG KTIDEVNTKA
     FEGTLLAHTD GGVPNMVVNI PQLDEETFGY VVYFFELACA MSGYQLGVNP FNQPGVEAYK
     QNMFALLGKP GFEDLKKELE ERL
 
 
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