G6PI_BORGP
ID G6PI_BORGP Reviewed; 530 AA.
AC Q660E3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BG0752;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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; CP000013; AAU07578.1; -; Genomic_DNA.
DR RefSeq; WP_011194026.1; NZ_CP028872.1.
DR AlphaFoldDB; Q660E3; -.
DR SMR; Q660E3; -.
DR STRING; 290434.BG0752; -.
DR PRIDE; Q660E3; -.
DR EnsemblBacteria; AAU07578; AAU07578; BG0752.
DR KEGG; bga:BG0752; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_12; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002276; Chromosome.
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..530
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180607"
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; 59951 MW; 9E5A80D17DD3BB83 CRC64;
MINYKNLNEL ENFKILEGIA PEVLKTALTG KRIKEYDITI EGDSVHYNYA SKQINENHLK
IFQNLSDEAN LIEKYKEVLN GEKINISENR KVLHHLTRGQ IGKDVIEDNK ENMREFFQSE
LEKIYNFAKQ VHSGNIKSVN GKKFKNVVQI GIGGSSLGPK ALYSSIKNYA KKHNLALMNG
YFISNIDPDE SEEVLNSINL DETLFIIVSK SGNTLETTAN MQFLINKLKS NGIKEYKKQM
TIITLKNSML ALEETGCLEY FFMHDSIGGR FSPTSAVGLA LLTLCFTEKI VKEIIKGANK
TDKKSLNKKV KDNAPLLAAL ISIYERNVLN YSSNCIIAYS KAMENFYLHL QQLEMESNGK
SVNRFNETIN YKTVRIIWGG VGTDVQHSFF QMLHQGTDIV PMDFIGFNAT QLKEDVISDN
SSSNDKLKAN LIAQIIAFSK GKENSNKNKN FKGERPSALI YSKELTPYAI GAILSHYENK
VMFEGFLLNI NSFDQEGVQL GKILANQILK NNAFEDEVIE SYSKKILKQD