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Database: UniProt
Entry: A0A0V0UWP0_9BILA
LinkDB: A0A0V0UWP0_9BILA
Original site: A0A0V0UWP0_9BILA 
ID   A0A0V0UWP0_9BILA        Unreviewed;       576 AA.
AC   A0A0V0UWP0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018388, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN   ORFNames=T09_15034 {ECO:0000313|EMBL:KRX55692.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX55692.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX55692.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX55692.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRX55692.1}.
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DR   EMBL; JYDN01000139; KRX55692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UWP0; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..576
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006870338"
SQ   SEQUENCE   576 AA;  64561 MW;  870BE0370B9AFAC9 CRC64;
     MALFLFCVTF SVVVDNCCST MALQTSLSSD RIYTELRTYV HNKGRHLNMK EMFESDPQRF
     EKFHLKLKCG KEEVLFDYSK NLINEELLEK LMSLARARKV EQVRQAMFSG QKINITEDRA
     VLHTALRNRS NTPILVDGKN VMGEVNRVLM QMKTFTDNVL TGKWLGCTGK QITDVVNIGI
     GGSDLGPLMV TEALKAYQQG PNVHFVSNID GTHLAETLKR LNPETTLFII ASKTFTTQET
     ITNAESAKEW FLSNVQNPEA VAKHFVALST NANKVKEFGI DPGNMFEFWD WVGGRYSLWS
     AIGLSIALFL GMDGFEQLLA GAHFMDEHFL QAPLEKNMPV IMAMLGILYI NFHGAETHAL
     LPYDQYLHRF AAYFQQGDME SNGKSVSKHG RRVDYATGPV VWGEPGTNGQ HAFYQLIHQG
     TRLIPCDFIL PIQSLNPIRN GLHHEILTAN FLAQTEALMR GKTENEVKME LKSAGMSDAA
     IGRLCPHKVF QGNRPSNSIV LTKLTPFTLG LLIAAYEHKI FVQGVIWDIN SFDQWGVELG
     KQLAKVIQPQ LKGTDTVTSH DSSTNGLINF IKTHKA
//
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