ID E3SCA0_9VIRI Unreviewed; 246 AA.
AC E3SCA0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=GPI {ECO:0000313|EMBL:ADB85504.1};
OS Closterium sp. EEC-2010.
OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC Desmidiales; Closteriaceae; Closterium.
OX NCBI_TaxID=707360 {ECO:0000313|EMBL:ADB85504.1};
RN [1] {ECO:0000313|EMBL:ADB85504.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20368268; DOI=10.1093/molbev/msq091;
RA Cocquyt E., Verbruggen H., Leliaert F., De Clerck O.;
RT "Evolution and cytological diversification of the green seaweeds
RT (Ulvophyceae).";
RL Mol. Biol. Evol. 27:2052-2061(2010).
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; GQ421564; ADB85504.1; -; mRNA.
DR AlphaFoldDB; E3SCA0; -.
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: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; IPR018189; Phosphoglucose_isomerase_CS.
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; PS00765; P_GLUCOSE_ISOMERASE_1; 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:ADB85504.1"
FT NON_TER 246
FT /evidence="ECO:0000313|EMBL:ADB85504.1"
SQ SEQUENCE 246 AA; 27577 MW; 2B423FFF99370C3D CRC64;
FAFWDWVGGR YSVTSAVGVL PLALQYGFDH VHKFLQGAWS IDTHFRTAHF HSNLPVLLGL
VSLWNVSFFN NPARAILPYC QALQKLAPHI QQVSMESNGK GVSMEGESLP YECGEIDFGE
PGTNGQHSFY QLTHQGRVVP CDFIGIIKSQ QSVYLKDEIV SNHDELMCNF FAQADALAYG
KTREELRAEG VPDYPIPHKT FTGNRPSLSI LLPSLTPYTV GQLLALYEHR VAVQGFVWGI
NSFDQW
//
