G6PI_LEGPL
ID G6PI_LEGPL Reviewed; 499 AA.
AC Q5WYE0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=lpl0796;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH15030.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5WYE0; -.
DR SMR; Q5WYE0; -.
DR PRIDE; Q5WYE0; -.
DR EnsemblBacteria; CAH15030; CAH15030; lpl0796.
DR KEGG; lpf:lpl0796; -.
DR LegioList; lpl0796; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002517; 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; 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.
FT CHAIN 1..499
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180662"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 383
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 487
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 499 AA; 56426 MW; 888C01CD7B641D93 CRC64;
MIRNSMKSHT ELLSWSLLQK EAKRVRLNSD SQPRVVPDSN NYESRKQINC IVYDYSRQRV
NRTIIDLLID LANEVKLPEK IDNLINGKKI NISENRPALH TALRDLSNKS ILIDGLDIMS
EVVSTREKIR MISNRIREKK WLGYSGLPIT DVVNIGIGGS DLGPRVCIHA LSNYVSKEFN
YHFISDVDPA SFNDVIVKIN PETTLFIVSS KSFTTKETLL NARKAFALYE DRASIDQHFI
AVTAHPERAH QIGIKTVLPI WDWVGGRFSF CSAVNLITAI AIGYEQFVEL LAGAHDVDTH
VQFTDFKNNI PVLMALIGIW NNNFLNIHNL LILTYSKKLE YFVPYVQQLD MESNGKSIDV
NGRMVGYATG PIVWGGLGNQ AQHSYFQLLC QGTHRCVGDF ITLKTNDEHE INSMCHYKMK
VLSEGIQTIE NPYGYIPGNM PMNHLILSDC SPYTLGALVA LYEHKIFVQS VIWNINPFDQ
PGIESAKSAH REITLSSEL