ID L7QQ64_9NEOP Unreviewed; 222 AA.
AC L7QQ64;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
DE Flags: Fragment;
OS Cecidoses eremita.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Incurvarioidea;
OC Cecidosidae; Cecidoses.
OX NCBI_TaxID=30230 {ECO:0000313|EMBL:AGB85511.1};
RN [1] {ECO:0000313|EMBL:AGB85511.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C., Mitter C., Solis M.A., Hayden J.E., Landry B., Nuss M.,
RA Simonsen T.J., Yen S.-H., Zwick A., Cummings M.P.;
RT "A molecular phylogeny for the pyraloid moths (Lepidoptera: Pyraloidea) and
RT its implications for higher-level classification.";
RL Syst. Entomol. 37:635-656(2012).
RN [2] {ECO:0000313|EMBL:AGB85511.1}
RP NUCLEOTIDE SEQUENCE.
RG LepTree.net;
RA Regier J.C.;
RT "Assembling the Tree of Life Lepidoptera.";
RL Submitted (MAR-2012) 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|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
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DR EMBL; JQ783701; AGB85511.1; -; mRNA.
DR AlphaFoldDB; L7QQ64; -.
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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05016; SIS_PGI_2; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 2: Evidence at transcript level;
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:AGB85511.1"
FT NON_TER 222
FT /evidence="ECO:0000313|EMBL:AGB85511.1"
SQ SEQUENCE 222 AA; 24308 MW; CE58E7AC0196767C CRC64;
GRYSLWSAIG LSIALHLGFN NFEKLLEGAS YMDEHFQTAP LEKNAPVILA VLGIWYSNFH
GAETHALLPY DQYMHRFAAY FQQGDMESNG KYVTRSGAEV GYSTGPIVWG EPGTNGQHAF
YQLIHQGTRI IPCDFIAPAQ SHNPISGGAH HQILLANFLA QTEALMTGKS EAQARAELEK
SGMAPEALAK ILPHKVFKGN RPTNSIVVRK VTPFTLGALI AM
//