G6PDC_SPIOL
ID G6PDC_SPIOL Reviewed; 574 AA.
AC O24357;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase, chloroplastic;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:Q43727};
DE Flags: Precursor;
GN Name=G6PD;
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].
RC STRAIN=cv. Matador; TISSUE=Leaf;
RA Fink A., Diogon T., Perroud P.F., Crespi P., Greppin H.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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 provide reducing power (NADPH) and pentose phosphates for fatty acid
CC and nucleic acid synthesis which are involved in membrane synthesis and
CC cell division. {ECO:0000250|UniProtKB:Q43727}.
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:0000250|UniProtKB:Q43727};
CC -!- ACTIVITY REGULATION: Regulated by metabolites. Post-translationally
CC inactivated by cysteine-mediated redox modification via the ferredoxin-
CC thioredoxin system in the light and this avoids futile cycles with
CC photosynthetic CO2 fixation (By similarity).
CC {ECO:0000250|UniProtKB:Q43839}.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11411}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ000182; CAA03939.1; -; mRNA.
DR PIR; T09088; T09088.
DR AlphaFoldDB; O24357; -.
DR SMR; O24357; -.
DR PRIDE; O24357; -.
DR UniPathway; UPA00115; UER00408.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProt.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chloroplast; Disulfide bond; Glucose metabolism;
KW NADP; Oxidoreductase; Plastid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..574
FT /note="Glucose-6-phosphate 1-dehydrogenase, chloroplastic"
FT /id="PRO_0000010439"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 93..100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 127
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 260..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT DISULFID 145..153
FT /note="Redox modulation"
FT /evidence="ECO:0000250|UniProtKB:Q43839"
SQ SEQUENCE 574 AA; 65180 MW; D498DB32D25849AA CRC64;
MEELVSCHHL PLLCLQSSVP PNGCLTFFQD SACQRCSHSE FSNGHPLNDV SLQNDVAVNP
IVAKSIDPSA DLQLLPLLES VKEEPTLSII VVGASGDLAK KKIFPALFAL FYENCLPENF
TVFGFSRTEM NDEELRTMIS KTLTCRIDQR ENCGEKMDHF LQRCFYHSGQ YNSEDDFSGL
DCKLKEKEAG RLQNRLFYLS IPPNIFVDVV RCVSHRASSA SGWTRVIVEK PFGRDSDSSR
ELTRSFKQYL SEDQIFRIDH YLGKELVENL SVLRFSNLVF EPLWSRNYIR NVQLIFSEDF
GTEGRGGYFD NYGIIRDIMQ NHLLQILALF AMETPVSLDA EDIRNEKVKV LRSMKPLKLQ
DVVVGQYKGH SKGNKSYSGY TDDPTVPNNS VTPTFAAAAL FIDNARWDGV PFLMKAGKAL
HTKRAEIRVQ FRHVPGNLYK KTFGTDLDKA TNELVLRVQP DEAIYLKINN KVPGLGMRLD
RTDLNLCYST RYRGEIPDAY ERLLLDAIEG ERRLFIRSDK LDAAWSLFTP LLKELEEKKV
APELYPYGSR GPVGAHYLAA KHNVRWGDLS GEDS
