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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 – 3791NADP By similarityBy similarity
Binding sitei548 – 5481NADP; via carbonyl oxygen By similarityBy similarity
Binding sitei548 – 5481Substrate By similarityBy similarity
Binding sitei616 – 6161Substrate By similarityBy similarity
Binding sitei635 – 6351Substrate By similarityBy similarity
Active sitei640 – 6401Proton acceptor; for G6PD activity By similarityBy similarity
Binding sitei745 – 7451Substrate By similarityBy similarity
Binding sitei779 – 7791Substrate By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi345 – 3528NADP By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 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-phosphogluconolactonase
Short name:
PfGluPho
Including the following 2 domains:
6-phosphogluconolactonase (EC:3.1.1.31)
Short name:
6PGL
Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
Short name:
G6PD
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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1701706-phosphogluconolactonaseAdd
BLAST
Regioni171 – 276106LinkerAdd
BLAST
Regioni277 – 910634Glucose-6-phosphate 1-dehydrogenaseAdd
BLAST
Regioni578 – 5825Substrate binding By similarityBy similarity

Sequence similaritiesi

In the C-terminal section; belongs to the glucose-6-phosphate dehydrogenase family.

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

« Hide

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

« 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 3D7.

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: May 14, 2014
This is version 75 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

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