G6PI_BURM1
ID G6PI_BURM1 Reviewed; 540 AA.
AC A9AJR8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Bmul_1357, BMULJ_01886;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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; CP000868; ABX15045.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG43806.1; -; Genomic_DNA.
DR RefSeq; WP_012213192.1; NC_010804.1.
DR AlphaFoldDB; A9AJR8; -.
DR SMR; A9AJR8; -.
DR STRING; 395019.Bmul_1357; -.
DR EnsemblBacteria; BAG43806; BAG43806; BMULJ_01886.
DR KEGG; bmj:BMULJ_01886; -.
DR KEGG; bmu:Bmul_1357; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_4; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008815; Chromosome 1.
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; Reference proteome.
FT CHAIN 1..540
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125702"
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; 59399 MW; 1A27BE526A2F770B CRC64;
MTLNSLPAWT ALQSHFEQIR HARLRDWFAP QNDPAPTRAE RFTFSGGGLA ADFSKNRITD
ETLRLLVQLA REARVEARRD AMFAGEIVNP TEGRAALHTA LRATDPHAPF HAQVSAERAK
MATFARAVRN GTWTGHTGKR IRHVINIGIG GSDLGPKMVT HALRHVATRD ISMHFVSNVD
GADLARVLEQ VDPEETLAIV VSKTFTTLET MTNARSLRDW FVAKGCPEDA LAKHFVGVSA
NPAEVVKFGI AADNVFEMWD WVGGRYSLWS AVGLSIMIAI GPEQFDELLA GANDMDRHFR
EAPLERNLPV LLGLIGIWYR NFFGSQSYLV APYSEALHYL PSYLQQLEME SNGKSARLDG
RFVDYPTAAV TWGEPGTNGQ HAFFQMLHQG PTIVPIDFIA VLTPEHPLAS HHPKLLANCF
AQSEALMLGR TLEEARKVAG PGKEDLAPHL TFPGNRPTTT LLVDALTPRS LGALIALYEH
KVLVQATVWD INPFDQWGVE LGKILGKVVE ADLAADALDT AKHDSSTTAL IARARAALKR