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Reviewed, UniProtKB/Swiss-Prot Q43727 (G6PD1_ARATH)

Last modified December 16, 2008. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic
      Short name=G6PDH1
      Short name=G6PD1
    EC=1.1.1.49
Gene names
Name: APG1
Ordered Locus Names: At5g35790
ORF Names: MIK22.2, MWP19.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length576 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.

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 structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast.

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.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Sequence caution

The sequence CAA59012.1 differs from that shown. Reason: Frameshift at position 65.

Ontologies

Keywords

   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt, oxidative branch

Inferred from direct assay. Source: TAIR

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Chloroplast Potential
Chain51 – 576526Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic
PRO_0000010435

Sites

Active site3261Proton acceptor By similarity
Binding site991NADP By similarity
Binding site1311NADP By similarity
Binding site2641Substrate By similarity
Binding site2681Substrate By similarity

Amino acid modifications

Disulfide bond149 ↔ 157Redox modulation By similarity

Experimental info

Sequence conflict1101A → D in CAA59012. Ref.5
Sequence conflict205 – 2139IPPNIFVDV → STPKLLVDE in CAA04696. Ref.1
Sequence conflict2971Q → E in CAA59012. Ref.5
Sequence conflict3831G → A in CAA59012. Ref.5
Sequence conflict485 – 4862RS → PR in CAA04696. Ref.1
Sequence conflict5141G → A in CAA04696. Ref.1
Sequence conflict5301D → E in CAA04696. Ref.1
Sequence conflict5391L → R in CAA04696. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q43727-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 6559FFCCF76F44DF

FASTA57665,428
        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 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for functional convergence of redox regulation in G6PDH isoforms of cyanobacteria and higher plants."
Wendt U.K., Hauschild R., Lange C., Pietersma M., Wenderoth I., von Schaewen A.
Plant Mol. Biol. 40:487-494(1999) [PubMed: 10437832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed: 9330910] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Nucleotide sequence of a cDNA encoding the glucose-6-phosphate dehydrogenase from Arabidopsis thaliana."
Fink A., Greppin H., Tacchini P.
(er) Plant Gene Register PGR95-021
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-576.
Strain: cv. Columbia.

Cross-references

Sequence databases

AJ001359 mRNA. Translation: CAA04696.1.
AB005236 Genomic DNA. Translation: BAB09918.1.
AY099561 mRNA. Translation: AAM20413.1.
BT002133 mRNA. Translation: AAN72144.1.
AY086213 mRNA. Translation: AAM64291.1.
X84230 mRNA. Translation: CAA59012.1. Frameshift.
RefSeqNP_198428.1.
UniGeneAt.60

3D structure databases

HSSPHSSP built from PDB template 1QKI based on UniProtKB P11413.
ModBaseSearch...

Proteomic databases

PRIDEQ43727.

Genome annotation databases

GeneID833559.
GenomeReviewsGene locus AT5G35790 in contig BA000015_GR.
KEGGath:AT5G35790.
NMPDRfig|3702.1.peg.25285.

Organism-specific databases

TAIRAt5g35790.

Gene expression databases

ArrayExpressQ43727.
GermOnlineAT5G35790. Arabidopsis thaliana.

Family and domain databases

InterProIPR001282. Glc-6-P_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR23429. G6PDH. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
ProDomPD001129. G6PD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PD1_ARATH
AccessionPrimary (citable) accession number: Q43727
Secondary accession number(s): O65577, Q9FFM5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 11, 2002
Last modified: December 16, 2008
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents