[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Matador; TISSUE=Leaf; Fink A., Diogon T., Perroud P.F., Crespi P., Greppin H.; Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
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

AJ000182; CAA03939.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09088; T09088.

3D structure databases

HSSP

P11413; 1QKI. [HSSP ENTRY / PDB]

ModBase

O24357.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004345;	Molecular function: glucose-6-phosphate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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

ProtoNet

O24357.

UniRef

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 ?`		`Chloroplast (Potential).`
`CHAIN`	`? 574`		`Glucose-6-phosphate 1-dehydrogenase, chloroplastic.`	`PRO_0000010439`
`ACT_SITE`	`322 322`		`Proton acceptor (By similarity).`
`BINDING`	`95 95`		`NADP (By similarity).`
`BINDING`	`127 127`		`NADP (By similarity).`
`BINDING`	`260 260`		`Substrate (By similarity).`
`BINDING`	`264 264`		`Substrate (By similarity).`
`BINDING`	`423 423`		`Substrate (By similarity).`
`DISULFID`	`145 153`		`Redox modulation (By similarity).`

Sequence information

Length: 574 AA [This is the length of the unprocessed precursor]

Molecular weight: 65180 Da [This is the MW of the unprocessed precursor]

CRC64: D498DB32D25849AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEELVSCHHL PLLCLQSSVP PNGCLTFFQD SACQRCSHSE FSNGHPLNDV SLQNDVAVNP 

        70         80         90        100        110        120 
IVAKSIDPSA DLQLLPLLES VKEEPTLSII VVGASGDLAK KKIFPALFAL FYENCLPENF 

       130        140        150        160        170        180 
TVFGFSRTEM NDEELRTMIS KTLTCRIDQR ENCGEKMDHF LQRCFYHSGQ YNSEDDFSGL 

       190        200        210        220        230        240 
DCKLKEKEAG RLQNRLFYLS IPPNIFVDVV RCVSHRASSA SGWTRVIVEK PFGRDSDSSR 

       250        260        270        280        290        300 
ELTRSFKQYL SEDQIFRIDH YLGKELVENL SVLRFSNLVF EPLWSRNYIR NVQLIFSEDF 

       310        320        330        340        350        360 
GTEGRGGYFD NYGIIRDIMQ NHLLQILALF AMETPVSLDA EDIRNEKVKV LRSMKPLKLQ 

       370        380        390        400        410        420 
DVVVGQYKGH SKGNKSYSGY TDDPTVPNNS VTPTFAAAAL FIDNARWDGV PFLMKAGKAL 

       430        440        450        460        470        480 
HTKRAEIRVQ FRHVPGNLYK KTFGTDLDKA TNELVLRVQP DEAIYLKINN KVPGLGMRLD 

       490        500        510        520        530        540 
RTDLNLCYST RYRGEIPDAY ERLLLDAIEG ERRLFIRSDK LDAAWSLFTP LLKELEEKKV 

       550        560        570 
APELYPYGSR GPVGAHYLAA KHNVRWGDLS GEDS

O24357 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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