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-AUG-2022, entry version 99.
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: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; 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
