[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Desiree; TISSUE=Green leaf; DOI=10.1104/pp.109.4.1327; PubMed=8539293 [NCBI, ExPASy, EBI, Israel, Japan] von Schaewen A., Langenkaemper G., Graeve K., Wenderoth I., Scheibe R.; "Molecular characterization of the plastidic glucose-6-phosphate dehydrogenase from potato in comparison to its cytosolic counterpart."; Plant Physiol. 109:1327-1335(1995).
[2]	ENZYME REGULATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-119; CYS-149; CYS-157; CYS-168; CYS-194 AND CYS-216. DOI=10.1074/jbc.272.43.26985; PubMed=9341136 [NCBI, ExPASy, EBI, Israel, Japan] Wenderoth I., Scheibe R., von Schaewen A.; "Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase."; J. Biol. Chem. 272:26985-26990(1997).

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.
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Plastid, chloroplast.
TISSUE SPECIFICITY: Green tissues, leaves and chloroplasts.
SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X83923; CAA58775.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T07375; T07375.

3D structure databases

HSSP

P11413; 1QKI. [HSSP ENTRY / PDB]

ModBase

Q43839.

Family and domain databases

InterPro

IPR001282; Glc-6-P_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR23429; G6PDH; 1.

Pfam

PF02781; G6PD_C; 1.
PF00479; G6PD_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000110; G6PD; 1.

PRINTS

PR00079; G6PDHDRGNASE.

ProDom

PD001129; G6PD; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00871; zwf; 1.

PROSITE

PS00069; G6P_DEHYDROGENASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Chloroplast; Glucose metabolism; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 63`	`63`	`Chloroplast (Potential).`
`CHAIN`	`64 577`	`514`	`Glucose-6-phosphate 1-dehydrogenase, chloroplastic.`	`PRO_0000010440`
`ACT_SITE`	`326 326`		`Proton acceptor (By similarity).`
`BINDING`	`131 131`		`NADP (By similarity).`
`BINDING`	`264 264`		`Substrate (By similarity).`
`BINDING`	`268 268`		`Substrate (By similarity).`
`BINDING`	`427 427`		`Substrate (By similarity).`
`DISULFID`	`149 157`		`Redox modulation.`
`MUTAGEN`	`119 119`		`C->S: No effect on redox regulation.`
`MUTAGEN`	`149 149`		`C->S: Abolishes redox regulation.`
`MUTAGEN`	`157 157`		`C->S: Abolishes redox regulation.`
`MUTAGEN`	`168 168`		`C->S: No effect on redox regulation.`
`MUTAGEN`	`194 194`		`C->S: No effect on redox regulation.`
`MUTAGEN`	`216 216`		`C->S: No effect on redox regulation.`

Sequence information

Length: 577 AA [This is the length of the unprocessed precursor]

Molecular weight: 65687 Da [This is the MW of the unprocessed precursor]

CRC64: A40B30EED2D87302 [This is a checksum on the sequence]

        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

Q43839 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools