G6PDC_TOBAC
ID G6PDC_TOBAC Reviewed; 593 AA.
AC Q43793;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
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;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun; TISSUE=Leaf;
RA Knight J.S., Emes M.J.;
RT "Isolation of a tobacco chloroplast glucose-6-phosphate dehydrogenase
RT cDNA.";
RL (er) Plant Gene Register PGR96-076(1996).
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 (By similarity). {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.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X99405; CAA67782.1; -; mRNA.
DR PIR; T03244; T03244.
DR RefSeq; NP_001313142.1; NM_001326213.1.
DR AlphaFoldDB; Q43793; -.
DR SMR; Q43793; -.
DR STRING; 4097.Q43793; -.
DR GeneID; 107828938; -.
DR KEGG; nta:107828938; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 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; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..593
FT /note="Glucose-6-phosphate 1-dehydrogenase, chloroplastic"
FT /id="PRO_0000010441"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 116..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 283..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT DISULFID 168..176
FT /note="Redox modulation"
FT /evidence="ECO:0000250|UniProtKB:Q43839"
SQ SEQUENCE 593 AA; 67369 MW; 228A7732E510E571 CRC64;
MVTLYSSPST HSSGPVASYS NSSIGLYNYH HNKQIAVSSI LSRKFGSLQI NQKPFWNAVR
MQDGAVATPP SKIENETPLK KLKNGILPVA PPKEQKDTID FDSNKAKSTV SITVVGASGD
LAKKKIFPAL FALYYEGCLP EHFTIFGYAR SKMTDAELRN MVSKTLTCRI DKRENCGEKM
EQFLERCFYH SGQYDSLENF AELDKKLKEH EAGRFSNRLF YLSIPPNIFI NAVRCASLSA
SSAHGWTRVI VEKPFGRDSE SSAALTRSLK QYLNEDQIFR IDHYLGKELV ENLSVLRFSN
LIFEPLWSRQ CIRNVQFIFS EDFGTEGRGG YFDHYGIIRD IMQNHLLQIL ALFAMETPVS
LDAEDIRNEK VKVLRSMRPL QLDDVIIGQY KCHTKGDVTY PGYTDDKTVP KDSLTPTFAA
AALFIDNARW DGVPFLMKAG KALHTRSAEI RVQFRHVPGN LYNKNFGSDL DQATNELVIR
VQPNEAIYLK INNKVPGLGM RLDRSNLNLL YSARYSKEIP DAYERLLLDA IEGERRLFIR
SDELDAAWSL FTPVLKELED KKIVPEYYPY GSRGPIGAHY LAARYKVRWG DLV
