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G8N4X7 (G8N4X7_GEOTH) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339

Short name=ATP-PFK HAMAP-Rule MF_00339
Short name=Phosphofructokinase HAMAP-Rule MF_00339
EC=2.7.1.11 HAMAP-Rule MF_00339
Alternative name(s):
Phosphohexokinase HAMAP-Rule MF_00339
Gene names
Name:pfkA HAMAP-Rule MF_00339
ORF Names:GTCCBUS3UF5_30850 EMBL AEV20387.1
OrganismGeobacillus thermoleovorans CCB_US3_UF5 [Complete proteome] EMBL AEV20387.1
Taxonomic identifier1111068 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339 SAAS SAAS022953

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate By similarity. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339 SAAS SAAS012828

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity SAAS SAAS022953 HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding92 – 932ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding122 – 1254ATP By similarity HAMAP-Rule MF_00339
Region41 – 455Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region145 – 1473Substrate binding By similarity HAMAP-Rule MF_00339
Region189 – 1913Substrate binding By similarity HAMAP-Rule MF_00339
Region205 – 2073Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region233 – 2353Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region269 – 2724Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1471Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1231Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site311ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1741Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1821Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2311Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2421Substrate By similarity HAMAP-Rule MF_00339
Binding site2631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
G8N4X7 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: 3A6C3DE2532BEA98

FASTA33936,525
        10         20         30         40         50         60 
MFKKTYEVGR VQFDANEVEM MKRIGVLTSG GDSPGMNAAI RAVVRKAIYH GVEVYGIYHG 

        70         80         90        100        110        120 
YAGLIAGNIK KLEVGDVGDI IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI 

       130        140        150        160        170        180 
GGDGSYQGAK KLTEHGFPCV GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH 

       190        200        210        220        230        240 
ERTYVVEVMG RHAGDIALWS GLAGGAETIL IPEADYDMDD IIARLKRGHE RGKKHSIIIV 

       250        260        270        280        290        300 
AEGVGSGVDF GRQIQEATGF ETRVTVLGHV QRGGSPTAFD RVLASRLGAR AVELLLEGKG 

       310        320        330 
GRCVGIQNNQ IVDHDIAEAL AKTHTVDQRM YTLSKELSI 

« Hide

References

[1]"Complete genome sequence of thermophilic Geobacillus thermoleovorans CCB_US3_UF5."
Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.
Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CCB_US3_UF5 EMBL AEV20387.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003125 Genomic DNA. Translation: AEV20387.1.
RefSeqYP_004983487.1. NC_016593.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEV20387; AEV20387; GTCCBUS3UF5_30850.
GeneID11627314.
KEGGgte:GTCCBUS3UF5_30850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

BioCycGTHE1111068:GJY8-3148-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG8N4X7_GEOTH
AccessionPrimary (citable) accession number: G8N4X7
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: July 9, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)