G6PI_LEIME
ID G6PI_LEIME Reviewed; 605 AA.
AC P42861;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Glucose-6-phosphate isomerase;
DE Short=GPI;
DE EC=5.3.1.9;
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
GN Name=PGI;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NHOM/BZ/84/BEL46;
RX PubMed=7870131; DOI=10.1016/0166-6851(94)00139-1;
RA Nyame K., Do Thi C.D., Opperdoes F.R., Michels P.A.M.;
RT "Subcellular distribution and characterization of glucosephosphate
RT isomerase in Leishmania mexicana mexicana.";
RL Mol. Biochem. Parasitol. 67:269-279(1994).
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;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR EMBL; X78206; CAA55042.1; -; Genomic_DNA.
DR PDB; 1Q50; X-ray; 2.60 A; A=44-604.
DR PDB; 1T10; X-ray; 2.35 A; A=1-605.
DR PDBsum; 1Q50; -.
DR PDBsum; 1T10; -.
DR AlphaFoldDB; P42861; -.
DR SMR; P42861; -.
DR VEuPathDB; TriTrypDB:LmxM.12.0530; -.
DR UniPathway; UPA00109; UER00181.
DR EvolutionaryTrace; P42861; -.
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-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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.
FT CHAIN 1..605
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180546"
FT ACT_SITE 410
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 441
FT /evidence="ECO:0000250"
FT ACT_SITE 569
FT /evidence="ECO:0000250"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:1T10"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 165..185
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 263..282
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 334..361
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 444..449
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:1Q50"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 471..488
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 492..501
FT /evidence="ECO:0007829|PDB:1T10"
FT TURN 508..512
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 513..516
FT /evidence="ECO:0007829|PDB:1T10"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 534..555
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 566..575
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:1T10"
FT HELIX 590..602
FT /evidence="ECO:0007829|PDB:1T10"
SQ SEQUENCE 605 AA; 67287 MW; 5C43210BF13FED71 CRC64;
MSDYFSKLKE HVVESTEING CTPSIATATF NAPYEVARKT KMLGVTDSSL LNLPAWKRLQ
SLYEKYGNDS ILSHFEKDHQ RFQRYSIEID LHSDDNFLFL DYSKSHINDE IKDALVALAE
ERGVRAFAKA MFDGQRVNST ENRAVLHVAL RNRSNRPIIV DGKDVMSDVN NVLAQMKDFT
ERVRSGEWKG QTGKSIYNIV NIGIGGSDLG PVMVTEALKP FSKRDLHCFF VSNVDGTHMA
EVLKQVNLEE TIFIIASKTF TTQETLTNAM SARNALMSYL KENGISTDGA VAKHFVALST
NTEKVREFGI DTVNMFAFWD WVGGRYSVWS AIGLSVMLSI GYDNFVEFLT GAHVMDNHFA
STPTEQNLPM MLALVGIWYN NFFGSETQAV LPYDQYLWRL PAYLQQLDME SNGKGVTKKS
GAVAVQTGPI VFGEAGTNGQ HAFYQLIHQG TKIIPCDFIG CVQTQNRVGD HHRTLMSNFF
AQTEALMVGK NAEEVRQELV KSGMSGDAIE NMIPHKTFTG SRPSNSILVN ALTPRALGAI
IAMYEHKVLV QGAIWGINSY DQWGVELGKV LAKSILPQLK SGNIVSDHDG STNGLINMFN
TRAHL
