ID Q6WAE7_ECOLX Unreviewed; 223 AA.
AC Q6WAE7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 83.
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:AAQ96100.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAQ96100.1};
RN [1] {ECO:0000313|EMBL:AAQ96100.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA157 {ECO:0000313|EMBL:AAQ96099.1}, TA234
RC {ECO:0000313|EMBL:AAQ96100.1}, and TA57 {ECO:0000313|EMBL:AAQ96102.1};
RX PubMed=14640415; DOI=10.1046/j.1420-9101.2003.00612.x;
RA Wertz J.E., Goldstone C., Gordon D.M., Riley M.A.;
RT "A molecular phylogeny of enteric bacteria and implications for a bacterial
RT species concept.";
RL J. Evol. Biol. 16:1236-1248(2003).
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|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
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DR EMBL; AY301205; AAQ96099.1; -; Genomic_DNA.
DR EMBL; AY301206; AAQ96100.1; -; Genomic_DNA.
DR EMBL; AY301208; AAQ96102.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WAE7; -.
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:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 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; 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 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:AAQ96100.1"
FT NON_TER 223
FT /evidence="ECO:0000313|EMBL:AAQ96100.1"
SQ SEQUENCE 223 AA; 25396 MW; D5348527FE86D637 CRC64;
IWYNNFFGAE TEAILPYDQY MHRFAAYFQQ GNMESNGKYV DRNGNVVDYQ TGPIIWGEPG
TNGQHAFYQL IHQGTKMVPC DFIAPAITHN PLSDHHQKLL SNFFAQTEAL AFGKSREVVE
QEYRDQGKDP ATLDYVVPFK VFEGNRPTNS ILLREITPFS LGALIALYEH KIFTQGVILN
IFTFDQWGVE LGKQLANRIL PELKDGKEIS SHDSSTNGLI NRY
//
