ID G9IYG0_EDWTA Unreviewed; 315 AA.
AC G9IYG0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-MAY-2023, entry version 47.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE Flags: Fragment;
GN Name=pgi {ECO:0000313|EMBL:AEW46502.1};
OS Edwardsiella tarda.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=636 {ECO:0000313|EMBL:AEW46502.1};
RN [1] {ECO:0000313|EMBL:AEW46502.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L-49231 {ECO:0000313|EMBL:AEW46502.1};
RX PubMed=22590641; DOI=10.1371/journal.pone.0036987;
RA Yang M., Lv Y., Xiao J., Wu H., Zheng H., Liu Q., Zhang Y., Wang Q.;
RT "Edwardsiella comparative phylogenomics reveal the new intra/inter-species
RT taxonomic relationships, virulence evolution and niche adaptation
RT mechanisms.";
RL PLoS ONE 7:e36987-E36987(2012).
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:0000256|ARBA:ARBA00029321,
CC ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
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DR EMBL; JN709558; AEW46502.1; -; Genomic_DNA.
DR AlphaFoldDB; G9IYG0; -.
DR UniPathway; UPA00109; UER00181.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; 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; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEW46502.1"
FT NON_TER 315
FT /evidence="ECO:0000313|EMBL:AEW46502.1"
SQ SEQUENCE 315 AA; 35126 MW; 5FA3B308BA4443FF CRC64;
TEDRAVLHIA LRNRSNTPIY VDGKDVMPEV NAVLAKMKQF CVRVIDGEWR GYTGKTITDV
VNIGIGGSDL GPYMVTEALR PYKNHLAMHF VSNVDGTHIA ETLQRLNPET TLFLVASKTF
TTQETMTNAH SARDWFLQAA GDERHVAKHF AALSTNAQAV AAFGIDTANM FEFWDWVGGR
YSLWSAIGLS IALSIGYDNF EQLLAGAHAM DRHFASAPLQ QNLPVLLALI GIWYNNFFGA
ETEAILPYDQ YMHRFPAYFQ QGNMESNGKY VDRNGQAVDY QTGPIIWGEP GTNGQHAFYQ
LIHQGTKLIP CDFIA
//