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Database: UniProt
Entry: Q6RZZ5_TRYCR
LinkDB: Q6RZZ5_TRYCR
Original site: Q6RZZ5_TRYCR 
ID   Q6RZZ5_TRYCR            Unreviewed;       397 AA.
AC   Q6RZZ5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   Name=Gpi {ECO:0000313|EMBL:AAR89395.1};
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693 {ECO:0000313|EMBL:AAR89395.1};
RN   [1] {ECO:0000313|EMBL:AAR89395.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CANIIIcl1 {ECO:0000313|EMBL:AAR89395.1};
RX   PubMed=16410006; DOI=10.1016/j.exppara.2005.11.014;
RA   Broutin H., Tarrieu F., Tibayrenc M., Oury B., Barnabe C.;
RT   "Phylogenetic analysis of the glucose-6-phosphate isomerase gene in
RT   Trypanosoma cruzi.";
RL   Exp. Parasitol. 113:1-7(2006).
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:0000256|ARBA:ARBA00029321,
CC         ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; AY484474; AAR89395.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6RZZ5; -.
DR   UniPathway; UPA00109; UER00181.
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   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW   ECO:0000256|RuleBase:RU000612};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAR89395.1"
FT   NON_TER         397
FT                   /evidence="ECO:0000313|EMBL:AAR89395.1"
SQ   SEQUENCE   397 AA;  44099 MW;  496FC234E432327E CRC64;
     FVDGNDVMHL VNKVLEQMKK LSEKVRRGEW KGQSGKPIRH VVNIGIGGSD LGPMMACEAL
     KPFSDRRISM HFVSNIDGTH LSEVLKLVDL ESTLFIIASK TFTTQETITN ALSARSEFLK
     FLSSRGIPEA GAVAKHFVAL STNAEKVKEF GIDEANMFQF WDWVGGRYSL WSAIGLSVMI
     SIGYDNFVEF LTGAHIMDEH FINAPTENNL PIILALVGIW YNNFFGSETQ AILPYDQYLW
     RLPAYLQQLD MESNGKGATK NGRMVSTHTG PIIFGEAGTN GQHAFYQLIH QGTKLIPCDF
     IGAIQTQNHI GEHHRILMSN FFAQTEALMI GKTPEEVKRE LESAGGKSED EIQLLIPQKT
     FTGGRPSNSL LVKALTPRAL GAIIAMYEHK VLVLLCI
//
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