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Q43839 (G6PDC_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate 1-dehydrogenase, chloroplastic

Short name=G6PD
EC=1.1.1.49
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. HAMAP-Rule MF_00966

Catalytic activity

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH. HAMAP-Rule MF_00966

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. HAMAP-Rule MF_00966

Subunit structure

Homodimer.

Subcellular location

Plastidchloroplast HAMAP-Rule MF_00966.

Tissue specificity

Green tissues, leaves and chloroplasts.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt, oxidative branch

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentchloroplast stroma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6363Chloroplast Potential
Chain64 – 577514Glucose-6-phosphate 1-dehydrogenase, chloroplastic HAMAP-Rule MF_00966
PRO_0000010440

Regions

Nucleotide binding97 – 1048NADP By similarity
Region264 – 2685Substrate binding By similarity

Sites

Active site3261Proton acceptor By similarity
Binding site1311NADP By similarity
Binding site2341NADP; via carbonyl oxygen By similarity
Binding site2341Substrate By similarity
Binding site3021Substrate By similarity
Binding site3211Substrate By similarity
Binding site4221Substrate By similarity
Binding site4631Substrate By similarity

Amino acid modifications

Disulfide bond149 ↔ 157Redox modulation Ref.2

Experimental info

Mutagenesis1191C → S: No effect on redox regulation. Ref.2
Mutagenesis1491C → S: Abolishes redox regulation. Ref.2
Mutagenesis1571C → S: Abolishes redox regulation. Ref.2
Mutagenesis1681C → S: No effect on redox regulation. Ref.2
Mutagenesis1941C → S: No effect on redox regulation. Ref.2
Mutagenesis2161C → S: No effect on redox regulation. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q43839 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A40B30EED2D87302

FASTA57765,687
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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.
PIRT07375.
RefSeqNP_001275038.1. NM_001288109.1.
UniGeneStu.18839.

3D structure databases

ProteinModelPortalQ43839.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ43839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102594145.
KEGGsot:102594145.

Phylogenomic databases

KOK00036.

Enzyme and pathway databases

UniPathwayUPA00115; UER00408.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00966. G6PD.
InterProIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23429. PTHR23429. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PDC_SOLTU
AccessionPrimary (citable) accession number: Q43839
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways