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P37830 (G6PD_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 89. 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, cytoplasmic isoform

Short name=G6PD
EC=1.1.1.49
Gene names
Name:G6PDH
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 generate NADPH for reductive biosyntheses. 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. HAMAP-Rule MF_00966

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

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00966.

Tissue specificity

Found in tubers, stolons, roots, and flower buds.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt, oxidative branch

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentchloroplast

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

Chain1 – 511511Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform HAMAP-Rule MF_00966
PRO_0000068101

Regions

Nucleotide binding36 – 438NADP By similarity
Region208 – 2125Substrate binding By similarity

Sites

Active site2701Proton acceptor By similarity
Binding site711NADP By similarity
Binding site1781NADP; via carbonyl oxygen By similarity
Binding site1781Substrate By similarity
Binding site2461Substrate By similarity
Binding site2651Substrate By similarity
Binding site3561Substrate By similarity
Binding site3611Substrate By similarity
Binding site3921Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P37830 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: BBD9E4891DA62671

FASTA51158,471
        10         20         30         40         50         60 
MAASWCIEKR GSIRNDSFRD NDNIPETGCL SIIVLGASGD LAKKKTFPAL FNLYRQGFLQ 

        70         80         90        100        110        120 
SNEVHIFGYA RTKISDDDLR SRIRGYLSQG KENEGEVSEF LQLIKYVSGS YDSAEGFTSL 

       130        140        150        160        170        180 
DKAISEHEFS KNSTEGSSRR LFYFALPPSV YPSVCRMIKS YCMNKSDLGG WTRTVVEKPF 

       190        200        210        220        230        240 
GKDLASSEQL SSQIGELFDE PQIYRIDHYL GKELVQNLLV LRFANRFFLP LWNRDNIDNI 

       250        260        270        280        290        300 
QIVFREDFGT EGRGGYFDEY GIIRDIIQNH LLQVLCLVAM EKPVSQKPEH IRDEKVKVLQ 

       310        320        330        340        350        360 
SMLPIEDEEV VLGQYEGYKD DPTVPNNSNT PTFATMVLRI HNERWEGVPF IMKAGKALNS 

       370        380        390        400        410        420 
RKAEIRVQFK DVPGDIFRCQ KQGRNEFVIR LQPSEAMYMK LTVKKPGLEM STVQSELDLS 

       430        440        450        460        470        480 
YGQRYQGVVI PEAYERLILD TIRGDQQHFV RRDELKAAWE IFTPLLHRID NGEVKPIPYK 

       490        500        510 
PGSRGPAEAD ELLQNAGYVQ THGYIWIPPT L 

« Hide

References

[1]"Purification, characterization, and cDNA sequence of glucose-6-phosphate dehydrogenase from potato (Solanum tuberosum L.)."
Graeve K., von Schaewen A., Scheibe R.
Plant J. 5:353-361(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Desiree.
Tissue: Green leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74421 mRNA. Translation: CAA52442.1.
PIRS60287.
UniGeneStu.18101.

3D structure databases

ProteinModelPortalP37830.
SMRP37830. Positions 31-507.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP37830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP37830.
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 nameG6PD_SOLTU
AccessionPrimary (citable) accession number: P37830
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 19, 2014
This is version 89 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