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Q27778

- PFKA_SCHMA

UniProt

Q27778 - PFKA_SCHMA

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Protein

ATP-dependent 6-phosphofructokinase

Gene

PFK

Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.1 PublicationUniRule annotation

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.2 PublicationsUniRule annotation

Cofactori

Magnesium.UniRule annotation

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.1 PublicationUniRule annotation

Kineticsi

  1. KM=3.5 mM for ATP1 Publication
  2. KM=0.8 mM for fructose 6-phosphate1 Publication

pH dependencei

Optimum pH is 7.5-9.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271ATP; via amide nitrogenUniRule annotation
Metal bindingi121 – 1211Magnesium; catalyticUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei203 – 2031Substrate; shared with dimeric partnerUniRule annotation
Binding sitei266 – 2661SubstrateUniRule annotation
Binding sitei294 – 2941Substrate; shared with dimeric partnerUniRule annotation
Binding sitei479 – 4791Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei575 – 5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei638 – 6381Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei664 – 6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei745 – 7451Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 912ATPUniRule annotation
Nucleotide bindingi120 – 1234ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fructose 6-phosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ27778.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PhosphofructokinaseUniRule annotation
Alternative name(s):
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFK
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 781781ATP-dependent 6-phosphofructokinasePRO_0000112033Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ27778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 394394N-terminal catalytic PFK domain 1Add
BLAST
Regioni166 – 1683Substrate bindingUniRule annotation
Regioni210 – 2123Substrate bindingUniRule annotation
Regioni300 – 3034Substrate bindingUniRule annotation
Regioni395 – 40915Interdomain linkerAdd
BLAST
Regioni410 – 781372C-terminal regulatory PFK domain 2Add
BLAST
Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni670 – 6734Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27778-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATWMEGKYV ARGQFTGECI AVLTSGGDAQ GMNAAVRAVV RMGIYCGCRV
60 70 80 90 100
FFIREGYQGL VDGGQNIQEA SWADVSGILQ LGGTKIGSAR CMDFRERYGR
110 120 130 140 150
LKAAENLVKN QITNLVVIGG DGSLTGANLF RAEWSSLLEE LVTSNKISAE
160 170 180 190 200
SAKQFHRLNI VGLVGSIDND FCGTDMTIGA DSALHRIIEA TDAISTTAHS
210 220 230 240 250
HQRCFILEVM GRHCGYLALV ASMACEADWV FIPEMPPTDD WREKLCHKLR
260 270 280 290 300
MNREHGQRVN IIMVAEGAID RACKPITCEI VKNLIVSELQ LDTRITVLGH
310 320 330 340 350
VQRGGSPSAF DRILGSRMGA EAVLALMDAD RDPNLPSCVI SLDGNQAVRV
360 370 380 390 400
PLVKCVDRTR QVAEAMKACD FDHAVELRGT SFMNNLATYI KLSKIEQPRQ
410 420 430 440 450
SVMSSENNLR IGIVNVGAPA CGINAVIRGF TRLGITKGYK VIGIHEGFSG
460 470 480 490 500
LVKGDASEIQ WADVRGWVGM GGSMLGTRRD TPNGLGIDKV AAKFKELKLS
510 520 530 540 550
GLLIIGGFEA YECMIELVEG REKYPELCIP MAMVPATISN NVPGTDFSLG
560 570 580 590 600
CDTALNEITS VLDKIKQSAL GTKRRVFVVE TMGGYCGYLA TMSALAGGAD
610 620 630 640 650
AAYIFEEPFT IDDLREDVVH LRAKIDDNVK RGLVLRADML INTITSEFIH
660 670 680 690 700
QLYAQEGQGI FDCRCNVLGH MQQGDRPSPF DRSLGTKFAS KAIDWLDEQI
710 720 730 740 750
NANIVQILQS IHQTFMLYIN WYCTSSDNLF KYSLELREHT DFVHRLPKEE
760 770 780
WWLSLRPLMR IMAKHDSLYE SESIMAGTDR K
Length:781
Mass (Da):86,060
Last modified:November 1, 1996 - v1
Checksum:iB2CDF20CAE926C38
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L31531 mRNA. Translation: AAA29911.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L31531 mRNA. Translation: AAA29911.1 .

3D structure databases

ProteinModelPortali Q27778.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK Q27778.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 2 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of a cDNA encoding phosphofructokinase from Schistosoma mansoni."
    Ding J., Su J.G.J., Mansour T.E.
    Mol. Biochem. Parasitol. 66:105-110(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
  2. "Purification, kinetics and inhibition by antimonials of recombinant phosphofructokinase from Schistosoma mansoni."
    Su J.G., Mansour J.M., Mansour T.E.
    Mol. Biochem. Parasitol. 81:171-178(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Entry informationi

Entry nameiPFKA_SCHMA
AccessioniPrimary (citable) accession number: Q27778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

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

External Data

Dasty 3