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Protein

Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic

Gene

APG1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei131 – 1311NADPBy similarity
Binding sitei234 – 2341NADP; via carbonyl oxygenBy similarity
Binding sitei234 – 2341SubstrateBy similarity
Binding sitei302 – 3021SubstrateBy similarity
Binding sitei321 – 3211SubstrateBy similarity
Active sitei326 – 3261Proton acceptorBy similarity
Binding sitei422 – 4221SubstrateBy similarity
Binding sitei427 – 4271SubstrateBy similarity
Binding sitei463 – 4631SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 1048NADPBy similarity

GO - Molecular functioni

  1. glucose-6-phosphate dehydrogenase activity Source: TAIR
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glucose metabolic process Source: TAIR
  2. pentose-phosphate shunt, oxidative branch Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.49. 399.
UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic (EC:1.1.1.49)
Short name:
G6PD1
Short name:
G6PDH1
Gene namesi
Name:APG1
Ordered Locus Names:At5g35790
ORF Names:MIK22.2, MWP19.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G35790.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050ChloroplastSequence AnalysisAdd
BLAST
Chaini51 – 576526Glucose-6-phosphate 1-dehydrogenase 1, chloroplasticPRO_0000010435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi149 ↔ 157Redox modulationBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ43727.
PRIDEiQ43727.

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

GenevestigatoriQ43727.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi18812. 3 interactions.
IntActiQ43727. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ43727.
SMRiQ43727. Positions 91-556.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 2685Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0364.
HOGENOMiHOG000046192.
InParanoidiQ43727.
KOiK00036.
OMAiNMISTTL.
PhylomeDBiQ43727.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q43727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATHSMIIPS PSSSSSSLAT AASPFKETLP LFSRSLTFPR KSLFSQVRLR
60 70 80 90 100
FFAEKHSQLD TSNGCATNFA SLQDSGDQLT EEHVTKGEST LSITVVGASG
110 120 130 140 150
DLAKKKIFPA LFALFYEGCL PQDFSVFGYA RTKLTHEELR DMISSTLTCR
160 170 180 190 200
IDQREKCGDK MEQFLKRCFY HSGQYNSEED FAELNKKLKE KEAGKISNRL
210 220 230 240 250
YYLSIPPNIF VDVVRCASLR ASSENGWTRV IVEKPFGRDS ESSGELTRCL
260 270 280 290 300
KQYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQLIF
310 320 330 340 350
SEDFGTEGRG GYFDQYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRSE
360 370 380 390 400
KVKVLRSMKP LRLEDVVVGQ YKGHNKGGKT YPGYTDDPTV PNHSLTPTFA
410 420 430 440 450
AAAMFINNAR WDGVPFLMKA GKALHTRGAE IRVQFRHVPG NLYKKSFATN
460 470 480 490 500
LDNATNELVI RVQPDEGIYL RINNKVPGLG MRLDRSDLNL LYRSRYPREI
510 520 530 540 550
PDAYERLLLD AIEGERRLFI RSDELDAAWD LFTPALKELE EKKIIPELYP
560 570
YGSRGPVGAH YLASKYNVRW GDLGEA
Length:576
Mass (Da):65,428
Last modified:July 11, 2002 - v2
Checksum:i6559FFCCF76F44DF
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101A → D in CAA59012 (Ref. 6) Curated
Sequence conflicti205 – 2139IPPNIFVDV → STPKLLVDE in CAA04696 (PubMed:10437832).Curated
Sequence conflicti297 – 2971Q → E in CAA59012 (Ref. 6) Curated
Sequence conflicti383 – 3831G → A in CAA59012 (Ref. 6) Curated
Sequence conflicti485 – 4862RS → PR in CAA04696 (PubMed:10437832).Curated
Sequence conflicti514 – 5141G → A in CAA04696 (PubMed:10437832).Curated
Sequence conflicti530 – 5301D → E in CAA04696 (PubMed:10437832).Curated
Sequence conflicti539 – 5391L → R in CAA04696 (PubMed:10437832).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001359 mRNA. Translation: CAA04696.1.
AB005236 Genomic DNA. Translation: BAB09918.1.
CP002688 Genomic DNA. Translation: AED94018.1.
AY099561 mRNA. Translation: AAM20413.1.
BT002133 mRNA. Translation: AAN72144.1.
AY086213 mRNA. Translation: AAM64291.1.
X84230 mRNA. Translation: CAA59012.1. Frameshift.
RefSeqiNP_198428.1. NM_122970.5.
UniGeneiAt.60.

Genome annotation databases

EnsemblPlantsiAT5G35790.1; AT5G35790.1; AT5G35790.
GeneIDi833559.
KEGGiath:AT5G35790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001359 mRNA. Translation: CAA04696.1.
AB005236 Genomic DNA. Translation: BAB09918.1.
CP002688 Genomic DNA. Translation: AED94018.1.
AY099561 mRNA. Translation: AAM20413.1.
BT002133 mRNA. Translation: AAN72144.1.
AY086213 mRNA. Translation: AAM64291.1.
X84230 mRNA. Translation: CAA59012.1. Frameshift.
RefSeqiNP_198428.1. NM_122970.5.
UniGeneiAt.60.

3D structure databases

ProteinModelPortaliQ43727.
SMRiQ43727. Positions 91-556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi18812. 3 interactions.
IntActiQ43727. 1 interaction.

Proteomic databases

PaxDbiQ43727.
PRIDEiQ43727.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G35790.1; AT5G35790.1; AT5G35790.
GeneIDi833559.
KEGGiath:AT5G35790.

Organism-specific databases

TAIRiAT5G35790.

Phylogenomic databases

eggNOGiCOG0364.
HOGENOMiHOG000046192.
InParanoidiQ43727.
KOiK00036.
OMAiNMISTTL.
PhylomeDBiQ43727.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.
BRENDAi1.1.1.49. 399.

Miscellaneous databases

PROiQ43727.

Gene expression databases

GenevestigatoriQ43727.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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].
  6. "Nucleotide sequence of a cDNA encoding the glucose-6-phosphate dehydrogenase from Arabidopsis thaliana."
    Fink A., Greppin H., Tacchini P.
    Plant Gene Register PGR95-021
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-576.
    Strain: cv. Columbia.

Entry informationi

Entry nameiG6PD1_ARATH
AccessioniPrimary (citable) accession number: Q43727
Secondary accession number(s): O65577, Q9FFM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 11, 2002
Last modified: April 29, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.