ID   G6PI_SYNY3              Reviewed;         531 AA.
AC   P52983;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=slr1349;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sakamoto T., Wada H., Nishida I., Ohta H., Murata N.;
RT   "Sequence analysis of a DNA fragment from Synechocystis PCC6803 containing
RT   genes homologous to cysE (serine acetyltransferase) and pgi (glucose-6-
RT   phosphate isomerase).";
RL   Plant Mol. Biol. 29:187-187(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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, ECO:0000305}.
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DR   EMBL; D13777; BAA02920.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18168.1; -; Genomic_DNA.
DR   PIR; S75607; S75607.
DR   AlphaFoldDB; P52983; -.
DR   SMR; P52983; -.
DR   IntAct; P52983; 2.
DR   STRING; 1148.1653253; -.
DR   PaxDb; P52983; -.
DR   EnsemblBacteria; BAA18168; BAA18168; BAA18168.
DR   KEGG; syn:slr1349; -.
DR   eggNOG; COG0166; Bacteria.
DR   InParanoid; P52983; -.
DR   OMA; CPAYAYG; -.
DR   PhylomeDB; P52983; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001425; 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; 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..531
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180755"
FT   ACT_SITE        324
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   531 AA;  58356 MW;  ABD5AA851C0BEF48 CRC64;
     MNNQQLWQRY QDWLYYHGGL DFYLDVSRMG FSDALVEDLQ PKFAKAFQDM VALEKGAIAN
     PDEQRMVGHY WLRNPALAPN DGIRAEITEP LRQIKAFVAD VHQGNIKPPT APKFTDLLAI
     GIGGSALGPQ FVAQALAPNF PPLAIHFIDN SDPDGIDRVL NCLKAQDKLK STLVVTTSKS
     GGTPEPRNGL AETKAVFEAQ GLHFADYAVA VTMPGSKLSQ QAQTEQWLQA FPMQDWVGGR
     TSELSAVGLL PAALQGIDIQ AMLDGAKTMD EATRVRELRQ NPAALLALAW YYAGDGQGKK
     DMVILPYKDR LLLFSRYLQQ LVMESLGKER DLDGNVVHQG IAVYGNKGST DQHAYVQQLR
     DGVPNFFATF IEVLHDRQGP SLELEPGVTS GDYLSGFLQG TRQALFENQR DSITVTIPEV
     DATSVGALIA LYERAVSFYG SLVNVNAYHQ PGVEAGKKAA ASILELQKAI LSTLQNESGP
     IALEALATKV QAPEQVETVY KIVRHLAAND RGVTLQGDRQ FPQRLQIQWR S