ID   G6PI_DESHY              Reviewed;         533 AA.
AC   Q24VW9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=DSY2034;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(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; AP008230; BAE83823.1; -; Genomic_DNA.
DR   RefSeq; WP_011460008.1; NC_007907.1.
DR   AlphaFoldDB; Q24VW9; -.
DR   SMR; Q24VW9; -.
DR   STRING; 138119.DSY2034; -.
DR   EnsemblBacteria; BAE83823; BAE83823; DSY2034.
DR   KEGG; dsy:DSY2034; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_033288_0_0_9; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001946; 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; 1.
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..533
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000252618"
FT   ACT_SITE        322
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        455
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   533 AA;  59487 MW;  A44A5D9D6FEF1AF6 CRC64;
     MVTITSWKRF KEYLYYDQEL GLLLDISRMN FSAEFLRSMA EPMREAYHQL QLLEKGALAN
     PDEGRMVGHY WLRNPDLAPT EEIVQDIKET LKEILDFAEQ IHSGRLQGEK GNPFRNILLV
     GVGGSILGPR FVADALASSR DKMKAFFIDN GDPDGIDRVL SRIGEELPAT LCLIISKSGG
     TIETRNGMLE VRRAYKEAGL SFPDHAVAIT QRGSQLDKLS QKEGWLRAFP MWDWVGGRTS
     LLSAVGLLSL ALQGIDVAGL LQGAKDCDGR TRRPDTLDNP GALLALMWYY STQGQGGKQM
     VVLPYKDRLE LFTKYLQQLI MESLGKEKNL QGETVHQGIT VYGNKGSSDQ HSYLQQLLEG
     PDNFFVTFIE VLKDRQGPST YMEENSTSGE YLQAFLLGTR EALTQKGRES LTITVKEVNA
     YTIGVLIALF ERAVSIYALL VGINAYHQPA VEMGKKAAGQ AIQLKNNIVE FLKSHPGKKF
     SVSELALAIQ EEEHQEMVFK LLLHLTTNPE HGVNMEPGEP WPESRFFVGG PIS