G6PI_FRATT
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 03-AUG-2022, entry version 89.
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=FTT_1315c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; 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}.
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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 OMA; IGVWYIN; -.
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; 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 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
