[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1023/A:1006257230779; PubMed=10437832 [NCBI, ExPASy, EBI, Israel, Japan] Wendt U.K., Hauschild R., Lange C., Pietersma M., Wenderoth I., von Schaewen A.; "Evidence for functional convergence of redox regulation in G6PDH isoforms of cyanobacteria and higher plants."; Plant Mol. Biol. 40:487-494(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/4.3.215; PubMed=9330910 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."; DNA Res. 4:215-230(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 17-576. STRAIN=cv. Columbia; Fink A., Greppin H., Tacchini P.; "Nucleotide sequence of a cDNA encoding the glucose-6-phosphate dehydrogenase from Arabidopsis thaliana."; (er) Plant Gene Register PGR95-021.

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.
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.
DEVELOPMENTAL STAGE: Increase of activity in the apex linked to the early stages of the transition from vegetative to reproductive growth.
MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase genes in A.thaliana.
SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
SEQUENCE CAUTION:
- Sequence=CAA59012.1; Type=Frameshift; Positions=65;

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

AJ001359; CAA04696.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB005236; BAB09918.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY099561; AAM20413.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002133; AAN72144.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086213; AAM64291.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X84230; CAA59012.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_198428.1; -.

UniGene

At.60

3D structure databases

HSSP

P11413; 1QKI. [HSSP ENTRY / PDB]

ModBase

Q43727.

Organism-specific databases

TAIR

At5g35790; -.

Gene expression databases

ArrayExpress

Q43727; -.

GermOnline

AT5G35790; Arabidopsis thaliana.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

GeneID

833559; -.

GenomeReviews

BA000015_GR; AT5G35790.

KEGG

ath:AT5G35790; -.

NMPDR

fig|3702.1.peg.25285; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 50`	`50`	`Chloroplast (Potential).`
`CHAIN`	`51 576`	`526`	`Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic.`	`PRO_0000010435`
`ACT_SITE`	`326 326`		`Proton acceptor (By similarity).`
`BINDING`	`99 99`		`NADP (By similarity).`
`BINDING`	`131 131`		`NADP (By similarity).`
`BINDING`	`264 264`		`Substrate (By similarity).`
`BINDING`	`268 268`		`Substrate (By similarity).`
`DISULFID`	`149 157`		`Redox modulation (By similarity).`
`CONFLICT`	`110 110`		`A -> D (in Ref. 5; CAA59012).`
`CONFLICT`	`205 213`		`IPPNIFVDV -> STPKLLVDE (in Ref. 1; CAA04696).`
`CONFLICT`	`297 297`		`Q -> E (in Ref. 5; CAA59012).`
`CONFLICT`	`383 383`		`G -> A (in Ref. 5; CAA59012).`
`CONFLICT`	`485 486`		`RS -> PR (in Ref. 1; CAA04696).`
`CONFLICT`	`514 514`		`G -> A (in Ref. 1; CAA04696).`
`CONFLICT`	`530 530`		`D -> E (in Ref. 1; CAA04696).`
`CONFLICT`	`539 539`		`L -> R (in Ref. 1; CAA04696).`

Sequence information

Length: 576 AA [This is the length of the unprocessed precursor]

Molecular weight: 65428 Da [This is the MW of the unprocessed precursor]

CRC64: 6559FFCCF76F44DF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATHSMIIPS PSSSSSSLAT AASPFKETLP LFSRSLTFPR KSLFSQVRLR FFAEKHSQLD 

        70         80         90        100        110        120 
TSNGCATNFA SLQDSGDQLT EEHVTKGEST LSITVVGASG DLAKKKIFPA LFALFYEGCL 

       130        140        150        160        170        180 
PQDFSVFGYA RTKLTHEELR DMISSTLTCR IDQREKCGDK MEQFLKRCFY HSGQYNSEED 

       190        200        210        220        230        240 
FAELNKKLKE KEAGKISNRL YYLSIPPNIF VDVVRCASLR ASSENGWTRV IVEKPFGRDS 

       250        260        270        280        290        300 
ESSGELTRCL KQYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQLIF 

       310        320        330        340        350        360 
SEDFGTEGRG GYFDQYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRSE KVKVLRSMKP 

       370        380        390        400        410        420 
LRLEDVVVGQ YKGHNKGGKT YPGYTDDPTV PNHSLTPTFA AAAMFINNAR WDGVPFLMKA 

       430        440        450        460        470        480 
GKALHTRGAE IRVQFRHVPG NLYKKSFATN LDNATNELVI RVQPDEGIYL RINNKVPGLG 

       490        500        510        520        530        540 
MRLDRSDLNL LYRSRYPREI PDAYERLLLD AIEGERRLFI RSDELDAAWD LFTPALKELE 

       550        560        570 
EKKIIPELYP YGSRGPVGAH YLASKYNVRW GDLGEA

Q43727 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