G6PI_BURP6
ID G6PI_BURP6 Reviewed; 540 AA.
AC A3NAH2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=BURPS668_2308;
OS Burkholderia pseudomallei (strain 668).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=668;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000570; ABN81484.1; -; Genomic_DNA.
DR RefSeq; WP_011851766.1; NC_009074.1.
DR AlphaFoldDB; A3NAH2; -.
DR SMR; A3NAH2; -.
DR EnsemblBacteria; ABN81484; ABN81484; BURPS668_2308.
DR KEGG; bpd:BURPS668_2308; -.
DR HOGENOM; CLU_017947_3_1_4; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002153; Chromosome I.
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..540
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000013950"
FT ACT_SITE 350
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 381
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 503
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 540 AA; 58789 MW; 80240EF650652BB6 CRC64;
MTLNSLPVWP ALQAHYEEIR DAHLRDWFAP ANDRAPTRAE RFTFEGGGLA ADFSKNRLTD
ATLALLVRLA REAGVEARRD AMFAGETVNP TEGRAALHTA LRANAADAPF QAQVAAERAK
MARFADAVRS GAWTGYTGKR IRHVVNIGIG GSDLGPKMVV HALHHVATPD IATHFVSNVD
GADLARVLER IDPEETLAII VSKTFTTLET MTNARSLRDW FVANGCPEGA LAKHFVGVSA
NPAEVVKFGI AEANVFEMWD WVGGRYSLWS AVGLSIMIAI GPERFDELLA GARDMDEHFR
TAPLERNLPA LQGLVGIWYR NFFGAQSYLV APYSEALHYL PSYLQQLEME SNGKSARIDG
AFVDYPTSAV TWGEPGTNGQ HAFFQMLHQG PTLVPIDFIA VLTPEHPLAS HHPKLLANCF
AQSEALMLGR TLDEARKIAG PAKPELAPHL TFPGNRPTTT LLVDALTPRT LGALIALYEH
KVLVQAAVWN INPFDQWGVE LGKILGKVVE ADLTAAQVDP AKHDSSTSAL IARARKALGE