ID   G6PI_RIPO1              Reviewed;         526 AA.
AC   B7JUF5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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}; OrderedLocusNames=PCC8801_0439;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001287; ACK64535.1; -; Genomic_DNA.
DR   RefSeq; WP_012593812.1; NC_011726.1.
DR   AlphaFoldDB; B7JUF5; -.
DR   SMR; B7JUF5; -.
DR   STRING; 41431.PCC8801_0439; -.
DR   EnsemblBacteria; ACK64535; ACK64535; PCC8801_0439.
DR   KEGG; cyp:PCC8801_0439; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_033288_0_0_3; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008204; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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; 2.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SSF53697; 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..526
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_1000135524"
FT   ACT_SITE        320
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        349
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        453
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   526 AA;  57479 MW;  F511F859D33DC37A CRC64;
     MDKLQLWQRY QNWLYYHEGL GIYLDISRMR FDDPFVDRLK PKFDKAFQDM EALEAGAIAN
     PDEGRMVGHY WLRAPELAPN DEARKEITEP LAAIADFVTK VHNTTIKPPT AEKFTDVLSI
     GIGGSALGPQ FVAEALSSDF PPMAIHFIDN SDPAGIDRIL TRLGDRLKST LVIVTSKSGG
     TPETRNGMLE VKAAYEAKGL DFAPHAVAVT MPGSKMDQFA ENWLARFPMQ DWVGGRTSEL
     SAVGLLPAAL QGIDIQAMLA GAKEMDVATR VKDLKTNPAA LLALAWYYSG NGKGEKDMVI
     LPYKDSLLLF SRYLQQLVME SLGKETDLDG NTVYQGIAVY GNKGSTDQHA YVQQLREGVP
     NFFATFIEVL EDRQGESIEL DPGITSGDYL SGFIQGTRQA LYENNRDSVT ITIPQVNPRI
     VGALIALYER TVSFYGSLVN VNAYHQPGVE AGKKMAASIL SLQTEIQKVI KESVGSLDLV
     TLAEKAGDPE AVEAVYKIVR HLAANGRGVT LDGDLANPSS LKVSAG