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P21777

- PFKA1_THET8

UniProt

P21777 - PFKA1_THET8

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Protein

ATP-dependent 6-phosphofructokinase 1

Gene
pfkA, TTHA1962
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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.2 Publications

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Allosterically activated by ADP and other diphosphonucleosides By similarity. Allosterically inhibited by phosphoenolpyruvate which induces the dissociation of the active tetramer into an inactive two-subunit forms.1 Publication

Kineticsi

  1. KM=0.08 mM for ATP1 Publication
  2. KM=0.025 mM for fructose 6-phosphate

pH dependencei

Optimum pH is 8.4.

Temperature dependencei

Optimum temperature is 85 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111ATP; via amide nitrogen By similarity
Metal bindingi103 – 1031Magnesium; catalytic By similarity
Active sitei128 – 1281Proton acceptor By similarity
Binding sitei155 – 1551Allosteric activator ADP By similarity
Binding sitei163 – 1631Substrate; shared with dimeric partner By similarity
Binding sitei212 – 2121Allosteric activator ADP By similarity
Binding sitei223 – 2231Substrate By similarity
Binding sitei246 – 2461Substrate; shared with dimeric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi72 – 732ATP By similarity
Nucleotide bindingi102 – 1054ATP By similarity

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB-HAMAP
  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-HAMAP
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

BioCyciTTHE300852:GH8R-2012-MONOMER.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase 1 (EC:2.7.1.11)
Short name:
ATP-PFK 1
Short name:
Phosphofructokinase 1
Alternative name(s):
Phosphohexokinase 1
Gene namesi
Name:pfkA
Ordered Locus Names:TTHA1962
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322ATP-dependent 6-phosphofructokinase 1UniRule annotationPRO_0000112001Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA1962.

Structurei

3D structure databases

ProteinModelPortaliP21777.
SMRiP21777. Positions 1-321.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Regioni126 – 1283Substrate binding By similarity
Regioni170 – 1723Substrate binding By similarity
Regioni186 – 1883Allosteric activator ADP binding By similarity
Regioni214 – 2163Allosteric activator ADP binding By similarity
Regioni252 – 2554Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000248869.
KOiK00850.
OMAiYRRGKLH.
OrthoDBiEOG644ZRM.
PhylomeDBiP21777.

Family and domain databases

HAMAPiMF_00339. Phosphofructokinase_I_B1.
InterProiIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21777-1 [UniParc]FASTAAdd to Basket

« Hide

MKRIGVFTSG GDAPGMNAAI RAVVRQAHAL GVEVIGIRRG YAGMIQGEMV    50
PLGVRDVANI IQRGGTILLT ARSQEFLTEE GRAKAYAKLQ AAGIEGLVAI 100
GGDGTFRGAL CLVEEHGMPV VGVPGTIDND LYGTDYTIGF DTAVNTALEA 150
IDRIRDTAAS HERVFFIEVM GRHAGFIALD VGLAGGAEVI AVPEEPVDPK 200
AVAEVLEASQ RRGKKSSIVV VAEGAYPGGA AGLLAAIREH LQVEARVTVL 250
GHIQRGGSPT AKDRILASRL GAAAVEALVG GASGVMVGEV EGEVDLTPLK 300
EAVERRKDIN RALLRLSQVL AL 322
Length:322
Mass (Da):33,537
Last modified:March 29, 2005 - v3
Checksum:i608CD4053E6ACEA3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111C → F in AAA27501. 1 Publication
Sequence conflicti273 – 2731A → P in AAA27501. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M71213 Genomic DNA. Translation: AAA27501.1.
AP008226 Genomic DNA. Translation: BAD71785.1.
RefSeqiYP_145228.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71785; BAD71785; BAD71785.
GeneIDi3169721.
KEGGittj:TTHA1962.
PATRICi23958903. VBITheThe93045_1933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M71213 Genomic DNA. Translation: AAA27501.1 .
AP008226 Genomic DNA. Translation: BAD71785.1 .
RefSeqi YP_145228.1. NC_006461.1.

3D structure databases

ProteinModelPortali P21777.
SMRi P21777. Positions 1-321.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1962.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71785 ; BAD71785 ; BAD71785 .
GeneIDi 3169721.
KEGGi ttj:TTHA1962.
PATRICi 23958903. VBITheThe93045_1933.

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000248869.
KOi K00850.
OMAi YRRGKLH.
OrthoDBi EOG644ZRM.
PhylomeDBi P21777.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci TTHE300852:GH8R-2012-MONOMER.

Family and domain databases

HAMAPi MF_00339. Phosphofructokinase_I_B1.
InterProi IPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 1 hit.
TIGRFAMsi TIGR02482. PFKA_ATP. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of phosphofructokinase 1 gene from a thermophilic bacterium, Thermus thermophilus."
    Xu J., Seki M., Denda K., Yoshida M.
    Biochem. Biophys. Res. Commun. 176:1313-1318(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Phosphoenolpyruvate-insensitive phosphofructokinase isozyme from Thermus thermophilus HB8."
    Xu J., Oshima T., Yoshida M.
    J. Biochem. 109:199-203(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25.
  4. "Allosteric nature of thermostable phosphofructokinase from an extreme thermophilic bacterium."
    Yoshida M.
    Biochemistry 11:1087-1093(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: HB8 / ATCC 27634 / DSM 579.
  5. "Tetramer-dimer conversion of phosphofructokinase from Thermus thermophilus induced by its allosteric effectors."
    Xu J., Oshima T., Yoshida M.
    J. Mol. Biol. 215:597-606(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiPFKA1_THET8
AccessioniPrimary (citable) accession number: P21777
Secondary accession number(s): Q5SGW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, 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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