ID   G6PI_BORBU              Reviewed;         530 AA.
AC   O51672;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 114.
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}; OrderedLocusNames=BB_0730;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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, ECO:0000305}.
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DR   EMBL; AE000783; AAC67084.2; -; Genomic_DNA.
DR   PIR; A70191; A70191.
DR   RefSeq; NP_212864.2; NC_001318.1.
DR   RefSeq; WP_002660427.1; NC_001318.1.
DR   AlphaFoldDB; O51672; -.
DR   SMR; O51672; -.
DR   STRING; 224326.BB_0730; -.
DR   PRIDE; O51672; -.
DR   EnsemblBacteria; AAC67084; AAC67084; BB_0730.
DR   KEGG; bbu:BB_0730; -.
DR   PATRIC; fig|224326.49.peg.1122; -.
DR   HOGENOM; CLU_017947_3_1_12; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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..530
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180606"
FT   ACT_SITE        356
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        502
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   530 AA;  60121 MW;  15C0F8B0CB6AE312 CRC64;
     MLNYKNLNEL ENFKILEGIA PEVLKTALTG KRIKEYDITI EGDSVHYNYA SKQINETHLK
     IFQNLSDEAN LIEKYKEVLD GEKINISENR KVLHHLTRGQ IGKDVIEDNK ENMREFFQSE
     LEKIYNFAKQ IHSGNIKSSN GKKFKNVVQI GIGGSSLGPK ALYSSIKNYA KKHNLALMNG
     YFISNIDPDE SEEVLSSINV DETLFIIVSK SGNTLETKAN MQFLINKLKL NGIKEYKKQM
     VIITLKDSML AIEEKGYLEY FFMHDSIGGR FSPTSAVGLT LLTLCFTEKV AKEILKGANE
     ADKKSLNKNV KDNASLLAAL ISIYERNVLN YSSNCIIAYS KAMENFYLHL QQLEMESNGK
     SVNRFNETIN YKTVRIIWGG IGTDVQHSFF QMLHQGTDIV PMDFIGFNET QLKEDVISDN
     SSSNDKLKAN LIAQIIAFSK GKENSNKNKN FQGERPSALI YSKELTPYAI GAILSHYENK
     VMFEGFLLNI NSFDQEGVQL GKIIANQILK NDNFKDEVIE SYSKKILKKF