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Q43839

- G6PDC_SOLTU

UniProt

Q43839 - G6PDC_SOLTU

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
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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: InterPro

    GO - Biological processi

    1. pentose-phosphate shunt, oxidative branch Source: EnsemblPlants/Gramene

    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

    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

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    MGVQLRLNPC SSSSAATSPS TFHNGTPYFC KKFNFLPFRT QPLNWVSGIY    50
    SRIQPRKHFE VFSSNGFPLN AVSVQDVQVP LTELGSGDTT VSITVIGASG 100
    DLAKKKILPA LFALFYEDCL PENFVVFGYS RTKLSDEELR NMISTTLTCR 150
    IDKRENCDAK MEHFLERCFY HSGQYNSEDD FAELDYKLKE KEGCRVSNRL 200
    FYLSIPPNIF VDVVRCASLK ASSTSGWTRV IVEKPFGRDL ESSSELTRSL 250
    KKYLTEEQIF RIDHYLGKEL VENLSVLRFS NLVFEPLWSR NYIRNVQFIF 300
    SEDFGTEGRG GYFDHYGIIR DIMQNHLLQI LALFAMETPV SLDAEDIRNE 350
    KVKVLRSMRP LQLEDVVLGQ YKGHSNGAKS YPAYTDDPTV PNGSITPTFS 400
    AAALFIDNAR WDGVPFLMKA GKALHTKRAE IRVQFRHVPG NLYKRNFGTD 450
    MDKATNELVL RLQPDEAIYL KINNKVPGLG MRLDRSDLNL LYKAKYRGEI 500
    PDAYERLLLD AIEGERRLFI RSDELDAAWA LFTPLLKELE EKKIAPELYP 550
    YGSRGPVGAH YLAAKHNVRW GDLSGDD 577
    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 1, 2014
    This is version 95 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