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Protein

Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic

Gene

At5g13110

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Miscellaneous

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

Catalytic activityi

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

Enzyme regulationi

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).By similarity

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic (At1g24280), Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic (APG1), Glucose-6-phosphate 1-dehydrogenase (At3g27300), Glucose-6-phosphate 1-dehydrogenase (AXX17_At3g29760), Glucose-6-phosphate 1-dehydrogenase (G6PD4), Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic (At5g13110), Glucose-6-phosphate 1-dehydrogenase (AXX17_At1g25530), Glucose-6-phosphate 1-dehydrogenase (At5g35790), Glucose-6-phosphate 1-dehydrogenase (AXX17_At5g33080), Glucose-6-phosphate 1-dehydrogenase (AXX17_At5g33080), Glucose-6-phosphate 1-dehydrogenase (AXX17_At5g12520), Glucose-6-phosphate 1-dehydrogenase (G6PD5), Glucose-6-phosphate 1-dehydrogenase (G6PD5), Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 2 (ACG12), Glucose-6-phosphate 1-dehydrogenase (At1g09420), Glucose-6-phosphate 1-dehydrogenase (AXX17_At5g38480), Glucose-6-phosphate 1-dehydrogenase (AXX17_At1g09330), Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform 1 (ACG9), Glucose-6-phosphate 1-dehydrogenase (At5g40760), Glucose-6-phosphate 1-dehydrogenase 4, chloroplastic (At1g09420)
  2. Probable 6-phosphogluconolactonase 5, chloroplastic (EMB2024), Probable 6-phosphogluconolactonase 3 (At5g24420), Probable 6-phosphogluconolactonase 4 (At5g24410), Probable 6-phosphogluconolactonase 1 (At1g13700), Probable 6-phosphogluconolactonase 2 (At3g49360)
  3. 6-phosphogluconate dehydrogenase, decarboxylating (AXX17_At5g39410), 6-phosphogluconate dehydrogenase, decarboxylating (AXX17_At3g01580), 6-phosphogluconate dehydrogenase, decarboxylating 2, chloroplastic (At5g41670), 6-phosphogluconate dehydrogenase, decarboxylating 3 (At3g02360), 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic (At1g64190), 6-phosphogluconate dehydrogenase, decarboxylating (AXX17_At1g57660)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei150NADPBy similarity1
Binding sitei253NADP; via carbonyl oxygenBy similarity1
Binding sitei253SubstrateBy similarity1
Binding sitei321SubstrateBy similarity1
Binding sitei340SubstrateBy similarity1
Active sitei345Proton acceptorBy similarity1
Binding sitei441SubstrateBy similarity1
Binding sitei446SubstrateBy similarity1
Binding sitei482SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi116 – 123NADPBy similarity8

GO - Molecular functioni

  • glucose-6-phosphate dehydrogenase activity Source: TAIR
  • NADP binding Source: InterPro

GO - Biological processi

  • glucose metabolic process Source: TAIR
  • pentose-phosphate shunt, oxidative branch Source: TAIR

Keywordsi

Molecular functionOxidoreductase
Biological processCarbohydrate metabolism, Glucose metabolism
LigandNADP

Enzyme and pathway databases

BRENDAi1.1.1.49 399
UniPathwayiUPA00115; UER00408

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic (EC:1.1.1.49)
Short name:
G6PD2
Short name:
G6PDH2
Gene namesi
Ordered Locus Names:At5g13110
ORF Names:T19L5_70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

AraportiAT5G13110
TAIRilocus:2179887 AT5G13110

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 59ChloroplastCombined sourcesAdd BLAST59
ChainiPRO_000001043660 – 596Glucose-6-phosphate 1-dehydrogenase 2, chloroplasticAdd BLAST537

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60N-acetylvalineCombined sources1
Disulfide bondi168 ↔ 176Redox modulationBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiQ9FY99
PRIDEiQ9FY99

PTM databases

iPTMnetiQ9FY99

Expressioni

Developmental stagei

Increase of activity in the apex linked to the early stages of the transition from vegetative to reproductive growth.

Gene expression databases

ExpressionAtlasiQ9FY99 baseline and differential
GenevisibleiQ9FY99 AT

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi16428, 2 interactors
IntActiQ9FY99, 1 interactor
STRINGi3702.AT5G13110.1

Structurei

3D structure databases

ProteinModelPortaliQ9FY99
SMRiQ9FY99
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni283 – 287Substrate bindingBy similarity5

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0563 Eukaryota
COG0364 LUCA
HOGENOMiHOG000046192
InParanoidiQ9FY99
KOiK00036
OMAiWRIATAD
OrthoDBiEOG093605BG
PhylomeDBiQ9FY99

Family and domain databases

HAMAPiMF_00966 G6PD, 1 hit
InterProiView protein in InterPro
IPR001282 G6P_DH
IPR019796 G6P_DH_AS
IPR022675 G6P_DH_C
IPR022674 G6P_DH_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR23429 PTHR23429, 1 hit
PfamiView protein in Pfam
PF02781 G6PD_C, 1 hit
PF00479 G6PD_N, 1 hit
PRINTSiPR00079 G6PDHDRGNASE
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00871 zwf, 1 hit
PROSITEiView protein in PROSITE
PS00069 G6P_DEHYDROGENASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FY99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALSSSVTT RSYHSGYLAS FSPVNGDRHR SLSFLSASPQ GLNPLDLCVR
60 70 80 90 100
FQRKSGRASV FMQDGAIVTN SNSSESKTSL KGLKDEVLSA LSQEAAKVGV
110 120 130 140 150
ESDGQSQSTV SITVVGASGD LAKKKIFPAL FALYYEGCLP EHFTIFGYSR
160 170 180 190 200
SKMTDVELRN MVSKTLTCRI DKRANCGEKM EEFLKRCFYH SGQYDSQEHF
210 220 230 240 250
TELDKKLKEH EAGRISNRLF YLSIPPNIFV DAVKCASTSA SSVNGWTRVI
260 270 280 290 300
VEKPFGRDSE TSAALTKSLK QYLEEDQIFR IDHYLGKELV ENLSVLRFSN
310 320 330 340 350
LIFEPLWSRQ YIRNVQFIFS EDFGTEGRGG YFDNYGIIRD IMQNHLLQIL
360 370 380 390 400
ALFAMETPVS LDAEDIRNEK VKVLRSMRPI RVEDVVIGQY KSHTKGGVTY
410 420 430 440 450
PAYTDDKTVP KGSLTPTFAA AALFIDNARW DGVPFLMKAG KALHTRSAEI
460 470 480 490 500
RVQFRHVPGN LYNRNTGSDL DQATNELVIR VQPDEAIYLK INNKVPGLGM
510 520 530 540 550
RLDRSNLNLL YSARYSKEIP DAYERLLLDA IEGERRLFIR SDELDAAWSL
560 570 580 590
FTPLLKEIEE KKRIPEYYPY GSRGPVGAHY LAAKHKVQWG DVSIDQ
Length:596
Mass (Da):67,160
Last modified:November 25, 2002 - v2
Checksum:iBDD89BEB49EF6E3B
GO

Sequence cautioni

The sequence CAC05439 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145I → V in CAA59011 (Ref. 4) Curated1
Sequence conflicti190H → I in CAA59011 (Ref. 4) Curated1
Sequence conflicti201T → I in CAA59011 (Ref. 4) Curated1
Sequence conflicti489L → F in CAA59011 (Ref. 4) Curated1
Sequence conflicti542D → G in AAL57678 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391711 Genomic DNA Translation: CAC05439.1 Sequence problems.
CP002688 Genomic DNA Translation: AED91851.1
AY065042 mRNA Translation: AAL57678.1
X84229 mRNA Translation: CAA59011.1
PIRiS71245
RefSeqiNP_196815.2, NM_121314.4
UniGeneiAt.61

Genome annotation databases

EnsemblPlantsiAT5G13110.1; AT5G13110.1; AT5G13110
GeneIDi831150
GrameneiAT5G13110.1; AT5G13110.1; AT5G13110
KEGGiath:AT5G13110

Similar proteinsi

Entry informationi

Entry nameiG6PD2_ARATH
AccessioniPrimary (citable) accession number: Q9FY99
Secondary accession number(s): Q43728, Q8VZD6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 25, 2002
Last modified: April 25, 2018
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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