Reviewed, UniProtKB/Swiss-Prot Q9FJI5 (G6PD6_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Protein existence	Evidence 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+ = D-glucono-1,5-lactone 6-phosphate + 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 process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt, oxidative branch Inferred from direct assay. Source: TAIR
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 515	515	Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 2		PRO_0000068098
Sites
	Binding site	40	1	NADP By similarity
	Binding site	73	1	NADP By similarity
	Binding site	212	1	Substrate By similarity
	Binding site	216	1	Substrate By similarity
Amino acid modifications
	Modified residue	18	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	361	1	A → S in CAB52675. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9FJI5-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: E8F7B88A52825C14	FASTA	515	59,116
	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

References

	« Hide 'large scale' referencesShow '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]	"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. , 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]	"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. 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. BT004633 mRNA. Translation: AAO42879.1.
IPI	IPI00539618.
PIR	T52610.
RefSeq	NP_198892.1.
UniGene	At.23901 Rra.24018
3D structure databases
SMR	Q9FJI5. Positions 33-511.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FJI5.
Proteomic databases
PRIDE	Q9FJI5.
Genome annotation databases
GeneID	834076.
GenomeReviews	Gene locus AT5G40760 in contig BA000015_GR.
KEGG	ath:AT5G40760.
NMPDR	fig|3702.1.peg.25780.
Organism-specific databases
TAIR	At5g40760.
Phylogenomic databases
HOGENOM	HBG322449.
InParanoid	Q9FJI5.
OMA	VVRGNAT.
PhylomeDB	Q9FJI5.
Enzyme and pathway databases
BRENDA	1.1.1.49. 302.
Gene expression databases
ArrayExpress	Q9FJI5.
Genevestigator	Q9FJI5.
GermOnline	AT5G40760. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001282. Glc-6-P_DH. IPR019796. Glc-6-P_DH_AS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR23429. G6PDH. 1 hit.
Pfam	PF02781. G6PD_C. 1 hit. PF00479. G6PD_N. 1 hit. [Graphical view]
PIRSF	PIRSF000110. G6PD. 1 hit.
PRINTS	PR00079. G6PDHDRGNASE.
TIGRFAMs	TIGR00871. zwf. 1 hit.
PROSITE	PS00069. G6P_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G6PD6_ARATH

Accession

Primary (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:	February 9, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)