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O24357 (G6PDC_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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
Gene names
Name:G6PD
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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 By similarity. 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

Homodimer By similarity. HAMAP-Rule MF_00966

Subcellular location

Plastidchloroplast By similarity HAMAP-Rule MF_00966.

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
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – ?Chloroplast Potential
Chain? – 574Glucose-6-phosphate 1-dehydrogenase, chloroplastic HAMAP-Rule MF_00966PRO_0000010439

Regions

Nucleotide binding93 – 1008NADP By similarity
Region260 – 2645Substrate binding By similarity

Sites

Active site3221Proton acceptor By similarity
Binding site1271NADP By similarity
Binding site2301NADP; via carbonyl oxygen By similarity
Binding site2301Substrate By similarity
Binding site2981Substrate By similarity
Binding site3171Substrate By similarity
Binding site4181Substrate By similarity
Binding site4591Substrate By similarity

Amino acid modifications

Disulfide bond145 ↔ 153Redox modulation By similarity

Sequences

Sequence LengthMass (Da)Tools
O24357 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D498DB32D25849AA

FASTA57465,180
        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 

« Hide

References

[1]Fink A., Diogon T., Perroud P.F., Crespi P., Greppin H.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Matador.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000182 mRNA. Translation: CAA03939.1.
PIRT09088.

3D structure databases

ProteinModelPortalO24357.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO24357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_SPIOL
AccessionPrimary (citable) accession number: O24357
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 86 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