ID L7JZW0_TRAHO Unreviewed; 530 AA.
AC L7JZW0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=THOM_0290 {ECO:0000313|EMBL:ELQ76576.1};
OS Trachipleistophora hominis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Trachipleistophora.
OX NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ76576.1, ECO:0000313|Proteomes:UP000011185};
RN [1] {ECO:0000313|EMBL:ELQ76576.1, ECO:0000313|Proteomes:UP000011185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA Embley T.M.;
RT "The genome of the obligate intracellular parasite Trachipleistophora
RT hominis: new insights into microsporidian genome dynamics and reductive
RT evolution.";
RL PLoS Pathog. 8:E1002979-E1002979(2012).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00024178}.
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; JH993832; ELQ76576.1; -; Genomic_DNA.
DR AlphaFoldDB; L7JZW0; -.
DR STRING; 72359.L7JZW0; -.
DR VEuPathDB; MicrosporidiaDB:THOM_0290; -.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; L7JZW0; -.
DR OMA; DWYRQLW; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000011185; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011185};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 270..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELQ76576.1"
SQ SEQUENCE 530 AA; 60903 MW; 6446D38B3F555C15 CRC64;
VFKYAEDFGD MVDRTLITLL DLFKNDPVRT EKFVRKVNVG DEAIYFDYSK THIDTMLLHE
LNRGFRSTET RKGMFKKEEL NFTEHRKVLH IALRDKNVLE AIEKNGSGDK LGEEEQLVFH
ELKKMRQFER KFEEGELLGV TGKKLRTVVN IGIGGSDLGP RMVTEALEFY KKDNVKVFYI
ANIDSTETER VFSKIDAEET LFIVVSKTFT TLETLANARL ALKLMKERLN VDEREITEKH
FVAVSANKEE VVNFGINNCF DMWDFVGGRF SLWSAVGLSI ILYIGFTNFL SLLKGASIMD
EHFKNEITEK NVPILQAYIE VYYTNFRKYE SRCVVAYDEY LKNLYLYLQQ LEMESNGKMA
TFSGSVSWNT GMVLWGGVGT SAQHSFFQLL HQGTRRVLVE FILPLQPLGD HKVMDHSHFE
MLFANCVAQS QALMVGTETS NNNKYFGGNR PSITICYTKL TPAVLGALIA FYEHKVFVQG
LYWRINSFDQ FGVELGKSLA KKVLEYIDDE PKDVDNSTKN LIELYKSLNK
//
