G6PI_PSEFL
ID G6PI_PSEFL Reviewed; 554 AA.
AC Q848I4;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
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};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Q8r1-96;
RA Mavrodi D.V., Weller D.M., Thomashow L.S.;
RT "A modified IVET system for plant-associated fluorescent Pseudomonas spp.";
RL Submitted (JAN-2003) 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; AY210414; AAO60163.1; -; Genomic_DNA.
DR STRING; 690597.JH730984_gene304; -.
DR PRIDE; Q848I4; -.
DR eggNOG; COG0166; Bacteria.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
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.
FT CHAIN 1..554
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180709"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 390
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 518
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 554 AA; 61526 MW; 8502AF3FB71A8DF5 CRC64;
MAYYRTPHDV TALPAWQALN DHRKAMQDFS MREAFNADPQ RFTQFTLSSC GLFLDYSKNL
INAQTRDLLV GLANEVDLKG AIKSLFEGEI VNASENRPAL HTALRRPVGD KLLVNGVNVM
PDVHKVLNQI TDLVGRIHDG LWRGYTEKPI TDVVNIGIGG SFLGPELVSE ALLSYAQKGV
RCHYLANIDG SEFHELTMKL RAETTLFIVS SKSFNTLETL KNAQAARAWY LAQGGSEAEL
YRHFIAVSSN NAAAVAFGIR EENIFPMWDW VGGRYSLWSA IGLPIALAIG MSNFKELLSG
AYSMDQHFQS APFEQNMPVL LALLGVWYGN FWGAQSHAIL PYDHYLRNIT KHLQQLDMES
NGKSVRQDGT PVSTDTGPVI WGGVGCNGQH AYHQLLHQGT QLIPADFIVP IVSFNPVSDH
HQWLYANCLS QSQALMLGKT RAEAEXELRD KGASEEEVQK LASHKVIPGN RPSNTLVVER
ISPRRLGALV ALYEHKVFVQ SVVWGINAFD QWGVELGKEL GKGVYNRLVG SEESLAEDAS
TQGLINYFRG RHRG