Reviewed, UniProtKB/Swiss-Prot Q43839 (G6PDC_SOLTU)

Names and origin

Protein names	Recommended name:     Glucose-6-phosphate 1-dehydrogenase, chloroplastic       Short name=G6PD     EC=1.1.1.49
Organism	Solanum tuberosum (Potato)
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division. May be involved in nitrite reduction.
Catalytic activity	D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH.
Enzyme regulation	Regulated by metabolites. Post-translationally inactivated by cysteine-mediated redox modification via the ferredoxin-thioredoxin system in the light and this avoids futile cycles with photosynthetic CO2 fixation. Ref.2
Pathway	Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subunit structure	Homodimer.
Subcellular location	Plastid › chloroplast.
Tissue specificity	Green tissues, leaves and chloroplasts.
Sequence similarities	Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro glucose-6-phosphate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 63	63	Chloroplast Potential
	Chain	64 – 577	514	Glucose-6-phosphate 1-dehydrogenase, chloroplastic		PRO_0000010440
Sites
	Active site	326	1	Proton acceptor By similarity
	Binding site	131	1	NADP By similarity
	Binding site	264	1	Substrate By similarity
	Binding site	268	1	Substrate By similarity
	Binding site	427	1	Substrate By similarity
Amino acid modifications
	Disulfide bond	149 ↔ 157		Redox modulation Ref.2
Experimental info
	Mutagenesis	119	1	C → S: No effect on redox regulation. Ref.2
	Mutagenesis	149	1	C → S: Abolishes redox regulation. Ref.2
	Mutagenesis	157	1	C → S: Abolishes redox regulation. Ref.2
	Mutagenesis	168	1	C → S: No effect on redox regulation. Ref.2
	Mutagenesis	194	1	C → S: No effect on redox regulation. Ref.2
	Mutagenesis	216	1	C → S: No effect on redox regulation. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q43839-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A40B30EED2D87302	FASTA	577	65,687
	10 20 30 40 50 60 MGVQLRLNPC SSSSAATSPS TFHNGTPYFC KKFNFLPFRT QPLNWVSGIY SRIQPRKHFE 70 80 90 100 110 120 VFSSNGFPLN AVSVQDVQVP LTELGSGDTT VSITVIGASG DLAKKKILPA LFALFYEDCL 130 140 150 160 170 180 PENFVVFGYS RTKLSDEELR NMISTTLTCR IDKRENCDAK MEHFLERCFY HSGQYNSEDD 190 200 210 220 230 240 FAELDYKLKE KEGCRVSNRL FYLSIPPNIF VDVVRCASLK ASSTSGWTRV IVEKPFGRDL 250 260 270 280 290 300 ESSSELTRSL KKYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQFIF 310 320 330 340 350 360 SEDFGTEGRG GYFDHYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRNE KVKVLRSMRP 370 380 390 400 410 420 LQLEDVVLGQ YKGHSNGAKS YPAYTDDPTV PNGSITPTFS AAALFIDNAR WDGVPFLMKA 430 440 450 460 470 480 GKALHTKRAE IRVQFRHVPG NLYKRNFGTD MDKATNELVL RLQPDEAIYL KINNKVPGLG 490 500 510 520 530 540 MRLDRSDLNL LYKAKYRGEI PDAYERLLLD AIEGERRLFI RSDELDAAWA LFTPLLKELE 550 560 570 EKKIAPELYP YGSRGPVGAH YLAAKHNVRW GDLSGDD

References

[1]	"Molecular characterization of the plastidic glucose-6-phosphate dehydrogenase from potato in comparison to its cytosolic counterpart." von Schaewen A., Langenkaemper G., Graeve K., Wenderoth I., Scheibe R. Plant Physiol. 109:1327-1335(1995) [PubMed: 8539293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Desiree. Tissue: Green leaf.
[2]	"Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase." Wenderoth I., Scheibe R., von Schaewen A. J. Biol. Chem. 272:26985-26990(1997) [PubMed: 9341136] [Abstract] Cited for: ENZYME REGULATION, DISULFIDE BOND, MUTAGENESIS OF CYS-119; CYS-149; CYS-157; CYS-168; CYS-194 AND CYS-216.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X83923 mRNA. Translation: CAA58775.1.
PIR	T07375.
3D structure databases
SMR	Q43839. Positions 91-572.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.49. 296.
Family and domain databases
InterPro	IPR001282. Glc-6-P_DH. IPR019796. Glc-6-P_DH_AS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR23429. G6PDH. 1 hit.
Pfam	PF02781. G6PD_C. 1 hit. PF00479. G6PD_N. 1 hit. [Graphical view]
PIRSF	PIRSF000110. G6PD. 1 hit.
PRINTS	PR00079. G6PDHDRGNASE.
TIGRFAMs	TIGR00871. zwf. 1 hit.
PROSITE	PS00069. G6P_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G6PDC_SOLTU

Accession

Primary (citable) accession number: Q43839

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)