G6PI_SPIOL
ID G6PI_SPIOL Reviewed; 566 AA.
AC O82059;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glucose-6-phosphate isomerase, cytosolic;
DE Short=GPI;
DE EC=5.3.1.9;
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
GN Name=PGIC; Synonyms=GPIS;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9651529; DOI=10.1016/s0378-1119(98)00229-7;
RA Nowitzki U., Flechner A., Kellermann J., Hasegawa M., Schnarrenberger C.,
RA Martin W.;
RT "Eubacterial origin of nuclear genes for chloroplast and cytosolic glucose-
RT 6-phosphate isomerase from spinach: sampling eubacterial gene diversity in
RT eukaryotic chromosomes through symbiosis.";
RL Gene 214:205-213(1998).
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;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR EMBL; AJ000266; CAA03983.1; -; mRNA.
DR PIR; T09154; T09154.
DR AlphaFoldDB; O82059; -.
DR SMR; O82059; -.
DR OrthoDB; 446616at2759; -.
DR SABIO-RK; O82059; -.
DR UniPathway; UPA00109; UER00181.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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 Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..566
FT /note="Glucose-6-phosphate isomerase, cytosolic"
FT /id="PRO_0000180568"
FT ACT_SITE 360
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 391
FT /evidence="ECO:0000250"
FT ACT_SITE 516
FT /evidence="ECO:0000250"
SQ SEQUENCE 566 AA; 62130 MW; 6079EE5D3A53460A CRC64;
MAPSTLICDT DSWQNLKTHV AEIKKTHLRD LMSDADRCKS MMVEFDGLLL DYSRQNATHD
TMSKLFQLAE ASHLKDKINQ MFNGEHINST ENRSVLHVAL RASRDAVING DGKNVVPDVW
QVLDKIRDFS EKIRSGSWVG VTGKPLTNVV AVGIGGSFLG PLFVHTALQT ESEAAECAKG
RQLRFLANVD PIDVAKNISG LNPETTLVVV VSKTFTTAET MLNARTLREW ISSALGPAAV
AKHMVAVSTN LTLVEKFGID PKNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFPIVEKFLK
GASSIDQHFH SAPLEKNLPV LLGLLSLWNV SFLGHPARAI LPYCQALEKF APHIQQVSME
SNGKGVSIDG VVLPFEAGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGI AKSQQPVYLK
GEVVSNHDEL MSNFFAQPDA LAYGKTQEEL QKENISPHLV PHKTFTGNRP SLSLLLPSLT
AYNVGQLLAI YEHRVAVEGF VWGINSFDQW GVELGKSLAN QVRKQLHASR TNGEAVKGFN
FSTTTVMAKY LQETSDVPAE LPTKLP