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Q43839

- G6PDC_SOLTU

UniProt

Q43839 - G6PDC_SOLTU

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Protein

Glucose-6-phosphate 1-dehydrogenase, chloroplastic

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 5 out of 5- 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. May be involved in nitrite reduction.

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.1 Publication

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 sitei463 – 4631SubstrateBy similarity

Regions

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

GO - Molecular functioni

  1. glucose-6-phosphate dehydrogenase activity Source: UniProtKB-EC
  2. NADP binding Source: EnsemblPlants/Gramene

GO - Biological processi

  1. isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: EnsemblPlants/Gramene
  2. pentose-phosphate shunt, oxidative branch Source: EnsemblPlants/Gramene
  3. photosynthesis Source: EnsemblPlants/Gramene
  4. protein autophosphorylation Source: EnsemblPlants/Gramene
  5. regulation of proton transport Source: EnsemblPlants/Gramene
  6. response to blue light Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase, chloroplastic (EC:1.1.1.49)
Short name:
G6PD
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. chloroplast stroma Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191C → S: No effect on redox regulation. 1 Publication
Mutagenesisi149 – 1491C → S: Abolishes redox regulation. 1 Publication
Mutagenesisi157 – 1571C → S: Abolishes redox regulation. 1 Publication
Mutagenesisi168 – 1681C → S: No effect on redox regulation. 1 Publication
Mutagenesisi194 – 1941C → S: No effect on redox regulation. 1 Publication
Mutagenesisi216 – 2161C → S: No effect on redox regulation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6363ChloroplastSequence AnalysisAdd
BLAST
Chaini64 – 577514Glucose-6-phosphate 1-dehydrogenase, chloroplasticPRO_0000010440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi149 ↔ 157Redox modulation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ43839.

Expressioni

Tissue specificityi

Green tissues, leaves and chloroplasts.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliQ43839.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK00036.

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.

Q43839-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVQLRLNPC SSSSAATSPS TFHNGTPYFC KKFNFLPFRT QPLNWVSGIY
60 70 80 90 100
SRIQPRKHFE VFSSNGFPLN AVSVQDVQVP LTELGSGDTT VSITVIGASG
110 120 130 140 150
DLAKKKILPA LFALFYEDCL PENFVVFGYS RTKLSDEELR NMISTTLTCR
160 170 180 190 200
IDKRENCDAK MEHFLERCFY HSGQYNSEDD FAELDYKLKE KEGCRVSNRL
210 220 230 240 250
FYLSIPPNIF VDVVRCASLK ASSTSGWTRV IVEKPFGRDL ESSSELTRSL
260 270 280 290 300
KKYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQFIF
310 320 330 340 350
SEDFGTEGRG GYFDHYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRNE
360 370 380 390 400
KVKVLRSMRP LQLEDVVLGQ YKGHSNGAKS YPAYTDDPTV PNGSITPTFS
410 420 430 440 450
AAALFIDNAR WDGVPFLMKA GKALHTKRAE IRVQFRHVPG NLYKRNFGTD
460 470 480 490 500
MDKATNELVL RLQPDEAIYL KINNKVPGLG MRLDRSDLNL LYKAKYRGEI
510 520 530 540 550
PDAYERLLLD AIEGERRLFI RSDELDAAWA LFTPLLKELE EKKIAPELYP
560 570
YGSRGPVGAH YLAAKHNVRW GDLSGDD
Length:577
Mass (Da):65,687
Last modified:November 1, 1996 - v1
Checksum:iA40B30EED2D87302
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83923 mRNA. Translation: CAA58775.1.
PIRiT07375.
RefSeqiNP_001275038.1. NM_001288109.1.
UniGeneiStu.18839.

Genome annotation databases

GeneIDi102594145.
KEGGisot:102594145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83923 mRNA. Translation: CAA58775.1 .
PIRi T07375.
RefSeqi NP_001275038.1. NM_001288109.1.
UniGenei Stu.18839.

3D structure databases

ProteinModelPortali Q43839.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q43839.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 102594145.
KEGGi sot:102594145.

Phylogenomic databases

KOi K00036.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00408 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00966. G6PD.
InterProi IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23429. PTHR23429. 1 hit.
Pfami PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000110. G6PD. 1 hit.
PRINTSi PR00079. G6PDHDRGNASE.
TIGRFAMsi TIGR00871. zwf. 1 hit.
PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of the plastidic glucose-6-phosphate dehydrogenase from potato in comparison to its cytosolic counterpart."
    von Schaewen A., Langenkaemper G., Graeve K., Wenderoth I., Scheibe R.
    Plant Physiol. 109:1327-1335(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Desiree.
    Tissue: Green leaf.
  2. "Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase."
    Wenderoth I., Scheibe R., von Schaewen A.
    J. Biol. Chem. 272:26985-26990(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, DISULFIDE BOND, MUTAGENESIS OF CYS-119; CYS-149; CYS-157; CYS-168; CYS-194 AND CYS-216.

Entry informationi

Entry nameiG6PDC_SOLTU
AccessioniPrimary (citable) accession number: Q43839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3