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Q8IKU0

- GLUPH_PLAF7

UniProt

Q8IKU0 - GLUPH_PLAF7

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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

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
Complete GO annotation...

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.
InParanoidiQ8IKU0.
KOiK00036.
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

« Hide

        10         20         30         40         50
MDYENFVKSA EEINNLHNVN YLETKDLNDF NWKAAYYICK EIYDKQQINK
60 70 80 90 100
DGYVVIGLSG GRTPIDVYKN MCLIKDIKID KSKLIFFIID ERYKSDDHKF
110 120 130 140 150
SNYNNIKFLF HNLNINEKEQ LYKPDTTKSI VDCILDYNDK IKIMIEKYKK
160 170 180 190 200
VDIAILGMGS DFHIASLFPN IFYNIYMNNY QNNYIYNEKT LDFINNDQDN
210 220 230 240 250
DNLKYLKEYV YFTTTNQFDV RKRITVSLNL LANASSKIFL LNSKDKLDLW
260 270 280 290 300
KNMLIKSYIE VNYNLYPATY LIDTSCTNEN VNINNNNNNN NKNKNNYCYS
310 320 330 340 350
NTTVISCGYE NYTKSIEEIY DSKYALSLYS NSLNKEELLT IIIFGCSGDL
360 370 380 390 400
AKKKIYPALF KLFCNNSLPK DLLIIGFART VQDFDTFFDK IVIYLKRCLL
410 420 430 440 450
CYEDWSISKK KDLLNGFKNR CRYFVGNYSS SESFENFNKY LTTIEEEEAK
460 470 480 490 500
KKYYATCYKM NGSDYNISNN VAEDNISIDD ENKTNEYFQM CTPKNCPDNV
510 520 530 540 550
FSSNYNFPYV INRMLYLALP PHIFVSTLKN YKKNCLNSKG TDKILLEKPF
560 570 580 590 600
GNDLDSFKML SKQILENFNE QQIYRIDHYL GKDMVSGLLK LKFTNTFLLS
610 620 630 640 650
LMNRHFIKCI KITLKETKGV YGRGQYFDPY GIIRDVMQNH MLQLLTLITM
660 670 680 690 700
EDPIDLNDES VKNEKIKILK SIPSIKLEDT IIGQYEKAEN FKEDENNDDE
710 720 730 740 750
SKKNHSYHDD PHIDKNSITP TFCTCILYIN SINWYGVPII FKSGKGLNKD
760 770 780 790 800
ICEIRIQFHN IMGSSDENMN NNEFVIILQP VEAIYLKMMI KKTGCEEMEE
810 820 830 840 850
VQLNLTVNEK NKKINVPEAY ETLLLECFKG HKKKFISDEE LYESWRIFTP
860 870 880 890 900
LLKELQEKQV KPLKYSFGSS GPKEVFGLVK KYYNYGKNYT HRPEFVRKSS
910
FYEDDLLDIN
Length:910
Mass (Da):106,987
Last modified:March 1, 2003 - v1
Checksum:i00BF883431E018A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q8IKU0.
KOi K00036.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 78 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