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Database: UniProt
Entry: A0A0V0TVC0_9BILA
LinkDB: A0A0V0TVC0_9BILA
Original site: A0A0V0TVC0_9BILA 
ID   A0A0V0TVC0_9BILA        Unreviewed;       601 AA.
AC   A0A0V0TVC0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
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   Name=GPI {ECO:0000313|EMBL:KRX42996.1};
GN   ORFNames=T05_6671 {ECO:0000313|EMBL:KRX42996.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42996.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX42996.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX42996.1};
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:KRX42996.1}.
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DR   EMBL; JYDJ01000130; KRX42996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TVC0; -.
DR   STRING; 144512.A0A0V0TVC0; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000055048; 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:UP000055048};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..601
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006869633"
SQ   SEQUENCE   601 AA;  67332 MW;  4F1A88501DF7B04A CRC64;
     MALFLFCVTF SVVVDDNSAN DLRHFWLAAN ISLSDLLFGV NCCSTMALQT SLSSDRIYTE
     LRTYVHNKGR HLNMKEMFES DPQRFEKFHL KLKCGKEEVL FDYSKNLINE ELLEKLMSLA
     RARKVEQVRQ AMFSGQKINI TEDRAVLHTA LRNRSNTPIL VDGKNVMGEV NRVLMQMKTF
     TDNVLTGKWL GCTGKQITDV VNIGIGGSDL GPLMVTEALK AYQQGPNVHF VSNIDGTHLA
     ETLKRLNPET TLFIIASKTF TTQETITNAE SAKEWFLSNV QNPEAVAKHF VALSTNANKV
     KEFGIDPGNM FEFWDWVGGR YSLWSAIGLS IALFLGMDGF EQLLAGAHFM DEHFLQAPLE
     KNMPVIMAML GILYINFHGA ETHALLPYDQ YLHRFAAYFQ QGDMESNGKS VSKHGRRVDY
     ATGPVVWGEP GTNGQHAFYQ LIHQGTRLIP CDFILPIQSL NPIRNGLHHE ILTANFLAQT
     EALMRGKTEN EVKMELKSAG MSDAAIGRLC PHKVFQGNRP SNSIVLTKLT PFTLGLLIAA
     YEHKIFVQGV IWDINSFDQW GVELGKQLAK VIQPQLKGTD TVTSHDSSTN GLINFIKTHK
     A
//
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