ID Q7DN41_9LILI Unreviewed; 567 AA.
AC Q7DN41;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 Name=Pgi {ECO:0000313|EMBL:BAA23178.1};
OS Dioscorea tokoro.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=64475 {ECO:0000313|EMBL:BAA23178.1};
RN [1] {ECO:0000313|EMBL:BAA23178.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9409845;
RA Terauchi R., Terachi T., Miyashita N.T.;
RT "DNA polymorphism at the Pgi locus of a wild yam, Dioscorea tokoro.";
RL Genetics 147:1899-1914(1997).
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
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DR EMBL; D88922; BAA23177.1; -; mRNA.
DR EMBL; D88923; BAA23178.1; -; mRNA.
DR AlphaFoldDB; Q7DN41; -.
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; 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 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}.
SQ SEQUENCE 567 AA; 62823 MW; B8F291E67CA533DA CRC64;
MATSTLICET PQWKDLNDHV EEIKKTHLRD LMQDSDRCKS MITEFDGIIL DYSRQRVLPA
TVEKLFQLAE VACLKQKIDR MYNGEKINCT ENRSVLHIAL RAARDKAIKS DDKNVVPDVW
HVLDKIKEFS ERIRSGSWVG ATGKALTDVV AVGIGGSFLG PLFVHTALQT DPEAAECAKG
RQLRFLANVD PIDVARSITG LNPETTLVVV VSKTFTTAET MLNARTLREW ISAALGPQAV
SKHMVAVSTN LTLVEKFGID PANAFAFWDW VGGRYSVCSA VGVLPLSLQY GFSVVHKFLN
GAASIDDHFH STPFEKNIPV LLGLLSVWNV SFLRYPARAI LPYSQALEKF APHIQQVSME
SNGKGVSIDG VPLPFETGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV MRSQQPIYLK
GEVVSNHDEL MSNFFAQPDA LAYGKVAEQL LNEKVPDHLI PHKTFPGNRP SLSLLLPSLN
AYNVGQLLAI YEHRIAVEGF VWGINSFDQW GVELGKSLAS QVRKQLHLSR TKAEPVEGFN
FSTTTLLTRY LEAETGVPSD QSQLPKL
//
