ID G6PI_FRATT Reviewed; 540 AA. AC Q5NFC4; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, 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}; GN OrderedLocusNames=FTT_1315c; OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=177416; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCHU S4 / Schu 4; RX PubMed=15640799; DOI=10.1038/ng1499; RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H., RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D., RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S., RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W., RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.; RT "The complete genome sequence of Francisella tularensis, the causative RT agent of tularemia."; RL Nat. Genet. 37:153-159(2005). 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}. 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; AJ749949; CAG45948.1; -; Genomic_DNA. DR RefSeq; WP_003022047.1; NZ_CP010290.1. DR RefSeq; YP_170268.1; NC_006570.2. DR PDB; 3LJK; X-ray; 1.48 A; A=1-540. DR PDB; 3M5P; X-ray; 1.65 A; A=1-540. DR PDB; 3Q7I; X-ray; 1.54 A; A=1-540. DR PDB; 3Q88; X-ray; 1.70 A; A=1-540. DR PDBsum; 3LJK; -. DR PDBsum; 3M5P; -. DR PDBsum; 3Q7I; -. DR PDBsum; 3Q88; -. DR AlphaFoldDB; Q5NFC4; -. DR SMR; Q5NFC4; -. DR IntAct; Q5NFC4; 2. DR STRING; 177416.FTT_1315c; -. DR EnsemblBacteria; CAG45948; CAG45948; FTT_1315c. DR KEGG; ftu:FTT_1315c; -. DR eggNOG; COG0166; Bacteria. DR OrthoDB; 140919at2; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; Q5NFC4; -. DR Proteomes; UP000001174; 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; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1..540 FT /note="Glucose-6-phosphate isomerase" FT /id="PRO_0000180644" FT ACT_SITE 346 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 377 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 505 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:3M5P" FT HELIX 6..12 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 18..24 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 50..62 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 65..74 FT /evidence="ECO:0007829|PDB:3LJK" FT TURN 80..83 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 88..92 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 106..125 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 150..158 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:3Q88" FT HELIX 177..184 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:3Q7I" FT HELIX 204..221 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 224..229 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 238..244 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:3Q7I" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 270..276 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 278..297 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 304..318 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 323..328 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 336..348 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 374..377 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 380..385 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 392..399 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 405..424 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 428..437 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 442..452 FT /evidence="ECO:0007829|PDB:3LJK" FT STRAND 460..466 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 470..491 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 499..501 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 502..516 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 521..525 FT /evidence="ECO:0007829|PDB:3LJK" FT HELIX 528..538 FT /evidence="ECO:0007829|PDB:3LJK" SQ SEQUENCE 540 AA; 61152 MW; 4D34257EBD77D2FD CRC64; MLFCDDSKKY LKEQNINLKN EFDKDDKRVE KFSLKHQNIY FDYSKNLIND YILKSLLESA EKSSLKDKIK QMFNGAKINS TEHRAVLHTA LRDLSSTPLI VDGQDIRQEV TKEKQRVKEL VEKVVSGRWR GFSGKKITDI VNIGIGGSDL GPKMVVRALQ PYHCTDLKVH FVSNVDADSL LQALHVVDPE TTLFIIASKS FSTEETLLNS ISAREWLLDH YEDEKAVANH FVAISSKLDK VKEFGIDLEH CYKMWDWVGG RYSLWSSIGM SIAFAIGYDN FEKLLAGAYS VDKHFKETEF SKNIPVIMAL LASYYSCTYN SQSQALLPYD ERLCYFVDYL QQADMESNGK SVNIAGETVN YQTGVVLWGG VGTNGQHAFH QLLHQGNIFI PVDFIAIATS HHNYDNHQQA LLANCFAQSQ ALMFGQSYDM VYNELLKSGL NETQAKELAA HKVIPGNRPS TTILLDELSP YSLGALIALY EHKIFVQGVL WDINSYDQWG VELGKKLGKN ILKAMNDDSS DEYQNLDDST RQLIAKVKNK //