ID G6PI_MYCBO Reviewed; 553 AA. AC P64193; A0A1R3XWX2; P77895; X2BGN2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 28-JAN-2026, entry version 103. 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=BQ2027_MB0971C; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LT708304; SIT99569.1; -; Genomic_DNA. DR RefSeq; WP_003404830.1; NC_002945.4. DR AlphaFoldDB; P64193; -. DR SMR; P64193; -. DR GeneID; 45424915; -. DR KEGG; mbo:BQ2027_MB0971C; -. DR PATRIC; fig|233413.5.peg.1056; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0048029; F:monosaccharide binding; IEA:TreeGrafter. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IEA:TreeGrafter. 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 FunFam; 3.40.50.10490:FF:000018; Glucose-6-phosphate isomerase; 1. DR Gene3D; 1.10.1390.10; -; 1. DR Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 2. 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 NCBIfam; NF001211; PRK00179.1; 1. DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR SUPFAM; SSF53697; SIS domain; 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..553 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_0000180673" FT REGION 524..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 541..553 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 357 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 388 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 514 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" SQ SEQUENCE 553 AA; 59974 MW; FB57DFFD16386AE4 CRC64; MTSAPIPDIT ATPAWDALRR HHDQIGNTHL RQFFADDPGR GRELTVSVGD LYIDYSKHRV TRETLALLID LARTAHLEER RDQMFAGVHI NTSEDRAVLH TALRLPRDAE LVVDGQDVVT DVHAVLDAMG AFTDRLRSGE WTGATGKRIS TVVNIGIGGS DLGPVMVYQA LRHYADAGIS ARFVSNVDPA DLIATLADLD PATTLFIVAS KTFSTLETLT NATAARRWLT DALGDAAVSR HFVAVSTNKR LVDDFGINTD NMFGFWDWVG GRYSVDSAIG LSLMTVIGRD AFADFLAGFH IIDRHFATAP LESNAPVLLG LIGLWYSNFF GAQSRTVLPY SNDLSRFPAY LQQLTMESNG KSTRADGSPV SADTGEIFWG EPGTNGQHAF YQLLHQGTRL VPADFIGFAQ PLDDLPTAEG TGSMHDLLMS NFFAQTQVLA FGKTAEEIAA DGTPAHVVAH KVMPGNRPST SILASRLTPS VLGQLIALYE HQVFTEGVVW GIDSFDQWGV ELGKTQAKAL LPVITGAGSP PPQSDSSTDG LVRRYRTERG RAG //