G6PD_SOLTU
ID G6PD_SOLTU Reviewed; 511 AA.
AC P37830;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000269|PubMed:8180621};
GN Name=G6PDH;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND PATHWAY.
RC STRAIN=cv. Desiree; TISSUE=Green leaf;
RX PubMed=8180621; DOI=10.1111/j.1365-313x.1994.00353.x;
RA Graeve K., von Schaewen A., Scheibe R.;
RT "Purification, characterization, and cDNA sequence of glucose-6-phosphate
RT dehydrogenase from potato (Solanum tuberosum L.).";
RL Plant J. 5:353-361(1994).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. The main function of this enzyme is
CC to generate NADPH for reductive biosyntheses.
CC {ECO:0000269|PubMed:8180621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000269|PubMed:8180621};
CC -!- ACTIVITY REGULATION: Regulated by metabolites.
CC {ECO:0000269|PubMed:8180621}.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000269|PubMed:8180621}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11413}.
CC -!- TISSUE SPECIFICITY: Found in tubers, stolons, roots, and flower buds.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X74421; CAA52442.1; -; mRNA.
DR PIR; S60287; S60287.
DR AlphaFoldDB; P37830; -.
DR SMR; P37830; -.
DR STRING; 4113.PGSC0003DMT400052250; -.
DR eggNOG; KOG0563; Eukaryota.
DR InParanoid; P37830; -.
DR SABIO-RK; P37830; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P37830; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..511
FT /note="Glucose-6-phosphate 1-dehydrogenase, cytoplasmic
FT isoform"
FT /id="PRO_0000068101"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 36..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 208..212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
SQ SEQUENCE 511 AA; 58471 MW; BBD9E4891DA62671 CRC64;
MAASWCIEKR GSIRNDSFRD NDNIPETGCL SIIVLGASGD LAKKKTFPAL FNLYRQGFLQ
SNEVHIFGYA RTKISDDDLR SRIRGYLSQG KENEGEVSEF LQLIKYVSGS YDSAEGFTSL
DKAISEHEFS KNSTEGSSRR LFYFALPPSV YPSVCRMIKS YCMNKSDLGG WTRTVVEKPF
GKDLASSEQL SSQIGELFDE PQIYRIDHYL GKELVQNLLV LRFANRFFLP LWNRDNIDNI
QIVFREDFGT EGRGGYFDEY GIIRDIIQNH LLQVLCLVAM EKPVSQKPEH IRDEKVKVLQ
SMLPIEDEEV VLGQYEGYKD DPTVPNNSNT PTFATMVLRI HNERWEGVPF IMKAGKALNS
RKAEIRVQFK DVPGDIFRCQ KQGRNEFVIR LQPSEAMYMK LTVKKPGLEM STVQSELDLS
YGQRYQGVVI PEAYERLILD TIRGDQQHFV RRDELKAAWE IFTPLLHRID NGEVKPIPYK
PGSRGPAEAD ELLQNAGYVQ THGYIWIPPT L
