ID V4Z938_TOXGV Unreviewed; 661 AA.
AC V4Z938;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
GN ORFNames=TGVEG_283780 {ECO:0000313|EMBL:ESS30496.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS30496.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESS30496.1}.
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DR EMBL; AAYL02000244; ESS30496.1; -; Genomic_DNA.
DR AlphaFoldDB; V4Z938; -.
DR STRING; 432359.V4Z938; -.
DR PaxDb; 5811-TGME49_083780; -.
DR EnsemblProtists; ESS30496; ESS30496; TGVEG_283780.
DR VEuPathDB; ToxoDB:TGVEG_283780; -.
DR eggNOG; KOG2446; Eukaryota.
DR OMA; DWYRQLW; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000002226; Partially assembled 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:UP000002226};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 661 AA; 74275 MW; 9768F1D43CFA861E CRC64;
MGARAFRGGR RPSMREVSCA TVHCARAVCL AATRCRFSRT RGRCRVPLKL AVCALFFLSE
VLLTFHFFCR ATGAFDGNRE DLDDFLHQSF FATDSFRRMA PTQLEQCASH GKLLQEKKKL
EKLHLRDLLK DEARNDLLIR STDQGVYLDF SRQKITLETL QHLVNLADER QVPAMVKRMF
SGEKINQTEN RAVLHVALRM PEGSEPVHVD GKNVLDEVHA VLRRIRVFSE KVRSGEIRGH
TGKKLVNVIS IGIGGSYLGT EFVHLALAAE GYAAEKAHGR QIHFLANVDP VDVWLAERGF
DPEETLVVVI SKTFTTAETM MNARSVRDWY LHHYKGDERA LGAHFCAVST NLDGTSKFGI
QSDRVFGFWD WVGGRYSVTS AVGILPLALQ YGYDVAQEFL NGAHAMDVHF KTAELADNLP
MLMGLISVWN ATFFGYSNVA VLPYAQALLR FPAHIQQLTM ESNGKRVTMD GKTLDFDVGE
IFFGEPGTNG QHSFYQLIHQ GRVIPAEFIG FCKSQRAIKL KEEPVSNHDE LMSNFFAQPD
ALAFGKTPEE LRKEGIPEKL VPHKTFPGDR PSCMLLFPEI SPFHIGQLLA LYEHRVAVEG
WLWGINSFDQ WGVELGKVLA KGVRGILQKR REGKAPHESG QSELCSSTRK ILEHYVQQSK
A
//
