ID   G6PI_ANADE              Reviewed;         550 AA.
AC   Q2IE39;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Adeh_3080;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC82849.1; -; Genomic_DNA.
DR   RefSeq; WP_011422131.1; NC_007760.1.
DR   AlphaFoldDB; Q2IE39; -.
DR   SMR; Q2IE39; -.
DR   STRING; 290397.Adeh_3080; -.
DR   EnsemblBacteria; ABC82849; ABC82849; Adeh_3080.
DR   KEGG; ade:Adeh_3080; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_7; -.
DR   OMA; IGVWYIN; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001935; 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   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; 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..550
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000252607"
FT   ACT_SITE        357
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        509
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   550 AA;  59816 MW;  03D0A07868C37B35 CRC64;
     MADRNDPLLR TPAWRALETH LAEVRPLHLR ELFARDPGRG DRLAAEGAGL YLDYSKQRVT
     EETVRLLVAL AEARGLPGRR AAMFRGEKVN ATEGRAALHV ALRAPRGERI EVDGKDVVPE
     VHAVLDRMAA FAEQVRSGAW TGFTGRRIRT VVNVGIGGSD LGPAMAYRAL RAYTTREIAF
     RFVSNVDGTD LAEAVRDLDP AETLFLVASK TFTTLETMTN AASARAWLLA ALGDERAVAR
     HFVAISTNEA EVRRFGIDPA NMFGFWDWVG GRYSMDSAIG LSTMIAVGPG GFRELLAGFR
     AMDEHFRDAP LERNLPALVG LIGVWNASLL GAETVAVLPY DQYLDRFPAY LQQLTMESNG
     KRVTASGAPV EGHGTGAIYW GEPGTNGQHS FYQLLHQGTH LVACDFIGFC RTLNPLGRHH
     DLLMANLFAQ GEALAFGKTA EEARAEGTPE ALVPHRTFPG NRPSSTILAD RLGPGTLGAL
     VALYEHAVFT QGVIWDVDSF DQWGVELGKV LANRIVKELE APADPALAHD GSTNALIRRY
     RARRGGSASS