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Q8IKU0

- GLUPH_PLAF7

UniProt

Q8IKU0 - GLUPH_PLAF7

Protein

Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonase

Gene

PF14_0511

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme which catalyzes the first two steps 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.1 Publication

    Catalytic activityi

    6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate.1 Publication
    D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.1 Publication

    Enzyme regulationi

    G6PD activity is inhibited by glucosamine-6-phosphate, NADPH, and 4-(4-bromophenyl)-7-(3,4-dimethoxyphenyl)-4,6,7,8-tetrahydroquinoline-2,5(1 H,3H)-dione. G6PD and 6PGL activities can be reversibly inhibited by S-glutathionylation (in vitro).1 Publication

    Kineticsi

    1. KM=19.2 µM for glucose-6-phosphate (at 25 degrees Celsius)1 Publication
    2. KM=6.5 µM for NADP+ (at 25 degrees Celsius)1 Publication
    3. KM=172 µM for 6-phosphoglucono-gamma-lactone (at 25 degrees Celsius)1 Publication

    Vmax=5.2 µmol/min/mg enzyme towards glucose-6-phosphate (at 25 degrees Celsius)1 Publication

    Vmax=4.6 µmol/min/mg enzyme towards NADP+ (at 25 degrees Celsius)1 Publication

    Vmax=46.6 µmol/min/mg enzyme with 6-phosphoglucono-gamma-lactone as substrate (at 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.0 for G6PD activity.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei379 – 3791NADPBy similarity
    Binding sitei548 – 5481NADP; via carbonyl oxygenBy similarity
    Binding sitei548 – 5481SubstrateBy similarity
    Binding sitei616 – 6161SubstrateBy similarity
    Binding sitei635 – 6351SubstrateBy similarity
    Active sitei640 – 6401Proton acceptor; for G6PD activityBy similarity
    Binding sitei745 – 7451SubstrateBy similarity
    Binding sitei779 – 7791SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi345 – 3528NADPBy similarity

    GO - Molecular functioni

    1. 6-phosphogluconolactonase activity Source: GeneDB_Pfalciparum
    2. glucose-6-phosphate dehydrogenase activity Source: GeneDB_Pfalciparum
    3. NADP binding Source: InterPro

    GO - Biological processi

    1. glucose 6-phosphate metabolic process Source: GeneDB_Pfalciparum
    2. pentose-phosphate shunt Source: GeneDB_Pfalciparum

    Keywords - Molecular functioni

    Hydrolase, Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00408.
    UPA00115; UER00409.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonase1 Publication
    Short name:
    PfGluPho1 Publication
    Including the following 2 domains:
    6-phosphogluconolactonase1 Publication (EC:3.1.1.311 Publication)
    Short name:
    6PGL1 Publication
    Glucose-6-phosphate 1-dehydrogenase1 Publication (EC:1.1.1.491 Publication)
    Short name:
    G6PD1 Publication
    Gene namesi
    ORF Names:PF14_0511
    OrganismiPlasmodium falciparum (isolate 3D7)
    Taxonomic identifieri36329 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)
    ProteomesiUP000001450: Chromosome 14

    Organism-specific databases

    EuPathDBiPlasmoDB:PF3D7_1453800.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 910910Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonasePRO_0000424558Add
    BLAST

    Keywords - PTMi

    Glutathionylation

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi5833.PF14_0511-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IKU0.
    SMRiQ8IKU0. Positions 1-320, 335-881.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1701706-phosphogluconolactonaseSequence AnalysisAdd
    BLAST
    Regioni171 – 276106LinkerSequence AnalysisAdd
    BLAST
    Regioni277 – 910634Glucose-6-phosphate 1-dehydrogenaseSequence AnalysisAdd
    BLAST
    Regioni578 – 5825Substrate bindingBy similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.Sequence Analysis
    In the C-terminal section; belongs to the glucose-6-phosphate dehydrogenase family.Sequence Analysis

    Phylogenomic databases

    HOGENOMiHOG000282031.
    KOiK00036.
    K01057.
    OMAiTPTFCTC.
    PhylomeDBiQ8IKU0.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    HAMAPiMF_00966. G6PD.
    InterProiIPR001282. G6P_DH.
    IPR022675. G6P_DH_C.
    IPR022674. G6P_DH_NAD-bd.
    IPR006148. Glc/Gal-6P_isomerase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR23429. PTHR23429. 1 hit.
    PfamiPF02781. G6PD_C. 1 hit.
    PF00479. G6PD_N. 2 hits.
    PF01182. Glucosamine_iso. 1 hit.
    [Graphical view]
    PRINTSiPR00079. G6PDHDRGNASE.

    Sequencei

    Sequence statusi: Complete.

    Q8IKU0-1 [UniParc]FASTAAdd to Basket

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    MDYENFVKSA EEINNLHNVN YLETKDLNDF NWKAAYYICK EIYDKQQINK    50
    DGYVVIGLSG GRTPIDVYKN MCLIKDIKID KSKLIFFIID ERYKSDDHKF 100
    SNYNNIKFLF HNLNINEKEQ LYKPDTTKSI VDCILDYNDK IKIMIEKYKK 150
    VDIAILGMGS DFHIASLFPN IFYNIYMNNY QNNYIYNEKT LDFINNDQDN 200
    DNLKYLKEYV YFTTTNQFDV RKRITVSLNL LANASSKIFL LNSKDKLDLW 250
    KNMLIKSYIE VNYNLYPATY LIDTSCTNEN VNINNNNNNN NKNKNNYCYS 300
    NTTVISCGYE NYTKSIEEIY DSKYALSLYS NSLNKEELLT IIIFGCSGDL 350
    AKKKIYPALF KLFCNNSLPK DLLIIGFART VQDFDTFFDK IVIYLKRCLL 400
    CYEDWSISKK KDLLNGFKNR CRYFVGNYSS SESFENFNKY LTTIEEEEAK 450
    KKYYATCYKM NGSDYNISNN VAEDNISIDD ENKTNEYFQM CTPKNCPDNV 500
    FSSNYNFPYV INRMLYLALP PHIFVSTLKN YKKNCLNSKG TDKILLEKPF 550
    GNDLDSFKML SKQILENFNE QQIYRIDHYL GKDMVSGLLK LKFTNTFLLS 600
    LMNRHFIKCI KITLKETKGV YGRGQYFDPY GIIRDVMQNH MLQLLTLITM 650
    EDPIDLNDES VKNEKIKILK SIPSIKLEDT IIGQYEKAEN FKEDENNDDE 700
    SKKNHSYHDD PHIDKNSITP TFCTCILYIN SINWYGVPII FKSGKGLNKD 750
    ICEIRIQFHN IMGSSDENMN NNEFVIILQP VEAIYLKMMI KKTGCEEMEE 800
    VQLNLTVNEK NKKINVPEAY ETLLLECFKG HKKKFISDEE LYESWRIFTP 850
    LLKELQEKQV KPLKYSFGSS GPKEVFGLVK KYYNYGKNYT HRPEFVRKSS 900
    FYEDDLLDIN 910
    Length:910
    Mass (Da):106,987
    Last modified:March 1, 2003 - v1
    Checksum:i00BF883431E018A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014187 Genomic DNA. Translation: AAN37124.1.
    PIRiS40259.
    S47533.
    RefSeqiXP_001348685.1. XM_001348649.2.

    Genome annotation databases

    EnsemblProtistsiPF14_0511:mRNA; PF14_0511:pep; PF14_0511.
    GeneIDi812093.
    KEGGipfa:PF14_0511.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014187 Genomic DNA. Translation: AAN37124.1 .
    PIRi S40259.
    S47533.
    RefSeqi XP_001348685.1. XM_001348649.2.

    3D structure databases

    ProteinModelPortali Q8IKU0.
    SMRi Q8IKU0. Positions 1-320, 335-881.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5833.PF14_0511-1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi PF14_0511:mRNA ; PF14_0511:pep ; PF14_0511 .
    GeneIDi 812093.
    KEGGi pfa:PF14_0511.

    Organism-specific databases

    EuPathDBi PlasmoDB:PF3D7_1453800.

    Phylogenomic databases

    HOGENOMi HOG000282031.
    KOi K00036.
    K01057.
    OMAi TPTFCTC.
    PhylomeDBi Q8IKU0.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00408 .
    UPA00115 ; UER00409 .

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    HAMAPi MF_00966. G6PD.
    InterProi IPR001282. G6P_DH.
    IPR022675. G6P_DH_C.
    IPR022674. G6P_DH_NAD-bd.
    IPR006148. Glc/Gal-6P_isomerase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR23429. PTHR23429. 1 hit.
    Pfami PF02781. G6PD_C. 1 hit.
    PF00479. G6PD_N. 2 hits.
    PF01182. Glucosamine_iso. 1 hit.
    [Graphical view ]
    PRINTSi PR00079. G6PDHDRGNASE.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Isolate 3D7.
    2. "Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: a unique bifunctional enzyme from Plasmodium falciparum."
      Jortzik E., Mailu B.M., Preuss J., Fischer M., Bode L., Rahlfs S., Becker K.
      Biochem. J. 436:641-650(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: Isolate 3D71 Publication.

    Entry informationi

    Entry nameiGLUPH_PLAF7
    AccessioniPrimary (citable) accession number: Q8IKU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 11, 2013
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, 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