ID G6PI_FRACC Reviewed; 556 AA.
AC Q2JH03;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=Francci3_0045;
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / HFP020203 / CcI3;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000249; ABD09439.1; -; Genomic_DNA.
DR RefSeq; WP_011434521.1; NZ_JENI01000001.1.
DR AlphaFoldDB; Q2JH03; -.
DR SMR; Q2JH03; -.
DR STRING; 106370.Francci3_0045; -.
DR KEGG; fra:Francci3_0045; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_11; -.
DR OrthoDB; 140919at2; -.
DR PhylomeDB; Q2JH03; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001937; 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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..556
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000252622"
FT ACT_SITE 363
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 394
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 522
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 556 AA; 60424 MW; 38F6F4CD01D177A1 CRC64;
MSTTEPAAPV APLDITATEE WAALTTHLRE ISEVSLRDLF AADPRRGETF AAEADGLYLD
YSKNRLTART VELLTALARR AGLADRIEAM FRGERINVTE NRPVLHVALR APAGTRIEVD
GVDVVPDVHR VLDAMSQFAD RVRSGDWLGA TGERIRTVVN IGIGGSDLGP AMAYDALRDY
ADRSIEVRFV SNVDPTDIWE ATADLDPAST LFIVSSKTFT TLETISNARA ARSWLTGLLG
EDAVSRHFVA VSTNAEKVAE FGIDTVNMFE FWDWVGGRYS VDCAIGLSLM IAIGPPNFRE
FLAGFAAMDT HFRTAPFERN LPVLLGLIGL WYRDFFGTAT HAVLPYSHYL GRFPAYLQQL
DMESNGKSVD LTGRPVSTPT GPIVWGTPGT NGQHAYYQLL HQGTTIVPAD FIGFVRPNHP
GVGTADGAGV DQHALLLANF LAQTEALAFG RTAAEVAAEG VTPDLVAHRT FPGNRPSNTL
LAQKLTPFAL GQLIALYEHK VFTQGVIWGI NSFDQWGVEL GKVLAGRIIP ELGSEQEPEL
GHDSSTNALI KRLRAG
//
