G6PDC_SOLTU
ID G6PDC_SOLTU Reviewed; 577 AA.
AC Q43839;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase, chloroplastic;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000269|PubMed:9341136};
DE Flags: Precursor;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Desiree; TISSUE=Green leaf;
RX PubMed=8539293; DOI=10.1104/pp.109.4.1327;
RA von Schaewen A., Langenkaemper G., Graeve K., Wenderoth I., Scheibe R.;
RT "Molecular characterization of the plastidic glucose-6-phosphate
RT dehydrogenase from potato in comparison to its cytosolic counterpart.";
RL Plant Physiol. 109:1327-1335(1995).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-119;
RP CYS-149; CYS-157; CYS-168; CYS-194 AND CYS-216.
RX PubMed=9341136; DOI=10.1074/jbc.272.43.26985;
RA Wenderoth I., Scheibe R., von Schaewen A.;
RT "Identification of the cysteine residues involved in redox modification of
RT plant plastidic glucose-6-phosphate dehydrogenase.";
RL J. Biol. Chem. 272:26985-26990(1997).
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:0000269|PubMed:9341136}.
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:9341136};
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. {ECO:0000269|PubMed:9341136}.
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:9341136}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11411}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:8539293}.
CC -!- TISSUE SPECIFICITY: Green tissues, leaves and chloroplasts.
CC {ECO:0000269|PubMed:8539293}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X83923; CAA58775.1; -; mRNA.
DR PIR; T07375; T07375.
DR RefSeq; NP_001275038.1; NM_001288109.1.
DR AlphaFoldDB; Q43839; -.
DR SMR; Q43839; -.
DR STRING; 4113.PGSC0003DMT400044818; -.
DR GeneID; 102594145; -.
DR KEGG; sot:102594145; -.
DR eggNOG; KOG0563; Eukaryota.
DR OrthoDB; 383995at2759; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q43839; baseline and differential.
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 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; Chloroplast; Disulfide bond; Glucose metabolism;
KW NADP; Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..577
FT /note="Glucose-6-phosphate 1-dehydrogenase, chloroplastic"
FT /id="PRO_0000010440"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 97..104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 234
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 264..268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT DISULFID 149..157
FT /note="Redox modulation"
FT /evidence="ECO:0000269|PubMed:9341136"
FT MUTAGEN 119
FT /note="C->S: No effect on redox regulation."
FT /evidence="ECO:0000269|PubMed:9341136"
FT MUTAGEN 149
FT /note="C->S: Abolishes redox regulation."
FT /evidence="ECO:0000269|PubMed:9341136"
FT MUTAGEN 157
FT /note="C->S: Abolishes redox regulation."
FT /evidence="ECO:0000269|PubMed:9341136"
FT MUTAGEN 168
FT /note="C->S: No effect on redox regulation."
FT /evidence="ECO:0000269|PubMed:9341136"
FT MUTAGEN 194
FT /note="C->S: No effect on redox regulation."
FT /evidence="ECO:0000269|PubMed:9341136"
FT MUTAGEN 216
FT /note="C->S: No effect on redox regulation."
FT /evidence="ECO:0000269|PubMed:9341136"
SQ SEQUENCE 577 AA; 65687 MW; A40B30EED2D87302 CRC64;
MGVQLRLNPC SSSSAATSPS TFHNGTPYFC KKFNFLPFRT QPLNWVSGIY SRIQPRKHFE
VFSSNGFPLN AVSVQDVQVP LTELGSGDTT VSITVIGASG DLAKKKILPA LFALFYEDCL
PENFVVFGYS RTKLSDEELR NMISTTLTCR IDKRENCDAK MEHFLERCFY HSGQYNSEDD
FAELDYKLKE KEGCRVSNRL FYLSIPPNIF VDVVRCASLK ASSTSGWTRV IVEKPFGRDL
ESSSELTRSL KKYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQFIF
SEDFGTEGRG GYFDHYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRNE KVKVLRSMRP
LQLEDVVLGQ YKGHSNGAKS YPAYTDDPTV PNGSITPTFS AAALFIDNAR WDGVPFLMKA
GKALHTKRAE IRVQFRHVPG NLYKRNFGTD MDKATNELVL RLQPDEAIYL KINNKVPGLG
MRLDRSDLNL LYKAKYRGEI PDAYERLLLD AIEGERRLFI RSDELDAAWA LFTPLLKELE
EKKIAPELYP YGSRGPVGAH YLAAKHNVRW GDLSGDD
