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Q9FJI5 (G6PD6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 2
EC=1.1.1.49
Alternative name(s):
G6PDH6
Short name=G6PD6
Gene names
Name:ACG12
Ordered Locus Names:At5g40760
ORF Names:K1B16.1, MNF13.6
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
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.

Catalytic activity

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

Enzyme regulation

Regulated by metabolites.

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

Cytoplasm.

Miscellaneous

There are 6 glucose-6-phosphate 1-dehydrogenase genes in A.thaliana.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

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

Inferred from direct assay. Source: TAIR

   Cellular componentcytosol

Inferred from direct assay. Source: TAIR

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from direct assay. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 2
PRO_0000068098

Sites

Binding site401NADP By similarity
Binding site731NADP By similarity
Binding site2121Substrate By similarity
Binding site2161Substrate By similarity

Amino acid modifications

Modified residue181Phosphoserine Ref.6

Experimental info

Sequence conflict3611A → S in CAB52675. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9FJI5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E8F7B88A52825C14

FASTA51559,116
        10         20         30         40         50         60 
MGSGQWHVEK RSTFRNDSFV REYGIVPETG CLSIIVLGAS GDLAKKKTFP ALFNLYRQGF 

        70         80         90        100        110        120 
LNPDEVHIFG YARTKISDEE LRDRIRGYLV DEKNAEQAEA LSKFLQLIKY VSGPYDAEEG 

       130        140        150        160        170        180 
FQRLDKAISE HEISKNSTEG SSRRLFYLAL PPSVYPSVCK MIKTCCMNKS DLGGWTRIVV 

       190        200        210        220        230        240 
EKPFGKDLES AEQLSSQIGE LFDESQIYRI DHYLGKELVQ NMLVLRFANR FFLPLWNRDN 

       250        260        270        280        290        300 
IENVQIVFRE DFGTEGRGGY FDEYGIIRDI IQNHLLQVLC LVAMEKPISL KPEHIRDEKV 

       310        320        330        340        350        360 
KVLQSVVPIS DDEVVLGQYE GYRDDDTVPN DSNTPTFATT ILRIHNERWE GVPFILKAGK 

       370        380        390        400        410        420 
ALNSRKAEIR IQFKDVPGDI FRCQKQGRNE FVIRLQPSEA MYMKLTVKQP GLDMNTVQSE 

       430        440        450        460        470        480 
LDLSYGQRYQ GVAIPEAYER LILDTIKGDQ QHFVRRDELK VAWEIFTPLL HRIDKGEVKS 

       490        500        510 
IPYKPGSRGP KEADQLLEKA GYLQTHGYIW IPPTL

« 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. VII. Sequence features of the regions of 1,013,767 bp covered by sixteen physically assigned P1 and TAC clones."
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., Tabata S.
DNA Res. 5:297-308(1998) [PubMed: 9872454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed: 9628582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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.
[6]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ010971 mRNA. Translation: CAB52675.1.
AB015470 Genomic DNA. Translation: BAB08837.1.
AB009052 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED94591.1.
BT004633 mRNA. Translation: AAO42879.1.
IPIIPI00539618.
PIRT52610.
RefSeqNP_198892.1. NM_123441.2.
UniGeneAt.23901.

3D structure databases

ProteinModelPortalQ9FJI5.
SMRQ9FJI5. Positions 30-513.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9FJI5.

Proteomic databases

PRIDEQ9FJI5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G40760.1; AT5G40760.1; AT5G40760.
GeneID834076.
GenomeReviewsGene locus AT5G40760 in contig BA000015_GR.
KEGGath:AT5G40760.
NMPDRfig|3702.1.peg.25780.

Organism-specific databases

TAIRAt5g40760.

Phylogenomic databases

GeneTreeEPGT00070000029608.
HOGENOMHBG322449.
InParanoidQ9FJI5.
OMAAEINNWR.
PhylomeDBQ9FJI5.
ProtClustDBPLN02539.

Gene expression databases

ArrayExpressQ9FJI5.
GenevestigatorQ9FJI5.
GermOnlineAT5G40760. Arabidopsis thaliana.

Family and domain databases

InterProIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00036.
PANTHERPTHR23429. G6PDH. 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 nameG6PD6_ARATH
AccessionPrimary (citable) accession number: Q9FJI5
Secondary accession number(s): Q9SUJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents