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Database: UniProt
Entry: G6PI_TRYBB
LinkDB: G6PI_TRYBB
Original site: G6PI_TRYBB 
ID   G6PI_TRYBB              Reviewed;         607 AA.
AC   P13377;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-MAY-2023, entry version 102.
DE   RecName: Full=Glucose-6-phosphate isomerase, glycosomal;
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   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=427;
RX   PubMed=2792108; DOI=10.1111/j.1432-1033.1989.tb15038.x;
RA   Marchand M., Kooystra U., Wierenga R.K., Lambeir A.-M., van Beeumen J.,
RA   Opperdoes F.R., Michels P.A.M.;
RT   "Glucosephosphate isomerase from Trypanosoma brucei. Cloning and
RT   characterization of the gene and analysis of the enzyme.";
RL   Eur. J. Biochem. 184:455-464(1989).
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   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Glycosome.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR   EMBL; X15540; CAA33547.1; -; Genomic_DNA.
DR   PIR; S06113; NUUTB.
DR   PDB; 2O2C; X-ray; 1.58 A; A/B/C=1-607.
DR   PDB; 2O2D; X-ray; 1.90 A; A/B/C=1-607.
DR   PDB; 3CV0; X-ray; 2.00 A; B=601-607.
DR   PDBsum; 2O2C; -.
DR   PDBsum; 2O2D; -.
DR   PDBsum; 3CV0; -.
DR   AlphaFoldDB; P13377; -.
DR   SMR; P13377; -.
DR   BRENDA; 5.3.1.9; 6520.
DR   SABIO-RK; P13377; -.
DR   UniPathway; UPA00109; UER00181.
DR   EvolutionaryTrace; P13377; -.
DR   GO; GO:0020015; C:glycosome; 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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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; 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; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW   Glycosome; Isomerase; Peroxisome.
FT   CHAIN           1..607
FT                   /note="Glucose-6-phosphate isomerase, glycosomal"
FT                   /id="PRO_0000180548"
FT   MOTIF           605..607
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        411
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        442
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        571
FT                   /evidence="ECO:0000250"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           54..66
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           71..77
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          98..107
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           110..122
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   TURN            140..143
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           148..151
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           167..185
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           210..218
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          227..232
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           237..246
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          252..257
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           264..283
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           292..295
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          296..301
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           303..309
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           313..315
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           332..334
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           335..341
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           343..362
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           365..367
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           369..382
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          388..394
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           396..398
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           401..413
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          431..433
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           439..442
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           445..450
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          457..464
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           472..489
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           493..502
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           508..514
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   TURN            515..518
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   STRAND          526..533
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           536..557
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           565..567
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           568..577
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           578..580
FT                   /evidence="ECO:0007829|PDB:2O2C"
FT   HELIX           592..604
FT                   /evidence="ECO:0007829|PDB:2O2C"
SQ   SEQUENCE   607 AA;  67518 MW;  AB237B7261CF2B74 CRC64;
     MSSYLDDLRI DLAASPASGG SASIAVGSFN IPYEVTRRLK GVGADADTTL TSCASWTQLQ
     KLYEQYGDEP IKKHFEADSE RGQRYSVKVS LGSKDENFLF LDYSKSHIND EIKCALLRLA
     EERGIRQFVQ SVFRGERVNT TENRPVLHIA LRNRSNRPIY VDGKDVMPAV NKVLDQMRSF
     SEKVRTGEWK GHTGKAIRHV VNIGIGGSDL GPVMATEALK PFSQRDLSLH FVSNVDGTHI
     AEVLKSIDIE ATLFIVASKT FTTQETITNA LSARRALLDY LRSRGIDEKG SVAKHFVALS
     TNNQKVKEFG IDEENMFQFW DWVGGRYSMW SAIGLPIMIS IGYENFVELL TGAHVIDEHF
     ANAPPEQNVP LLLALVGVWY INFFGAVTHA ILPYDQYLWR LPAYLQQLDM ESNGKYVTRS
     GKTVSTLTGP IIFGEAGTNG QHAFYQLIHQ GTNLIPCDFI GAIQSQNKIG DHHKIFMSNF
     FAQTEALMIG KSPSEVRREL EAAGERSAEK INALLPHKTF IGGRPSNTLL IKSLTPRALG
     AIIAMYEHKV LVQGAIWGID SYDQWGVELG KVLAKSILPQ LRPGMRVNNH DSSTNGLINM
     FNELSHL
//
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