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G8UIG9 (G8UIG9_TANFA) 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
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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 EMBL AEW22384.1
Ordered Locus Names:BFO_1157 EMBL AEW22384.1
OrganismTannerella forsythia (strain ATCC 43037 / JCM 10827 / FDC 338) (Bacteroides forsythus) [Complete proteome] [HAMAP] EMBL AEW22384.1
Taxonomic identifier203275 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeTannerella

Protein attributes

Sequence length336 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 HAMAP-Rule MF_00339 SAAS SAAS022953.

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 binding85 – 862ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding115 – 1184ATP By similarity HAMAP-Rule MF_00339
Region34 – 385Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region139 – 1413Substrate binding By similarity HAMAP-Rule MF_00339
Region183 – 1853Substrate binding By similarity HAMAP-Rule MF_00339
Region199 – 2013Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region227 – 2293Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region266 – 2694Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1411Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1161Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site241ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1681Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1761Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2251Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2361Substrate By similarity HAMAP-Rule MF_00339
Binding site2601Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
G8UIG9 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: D005340F009D9E0B

FASTA33636,204
        10         20         30         40         50         60 
MGFKLIRSNM STKIKCIGLL TSGGDAPGMN AAIRAVTRTA IYNGMAVKGI YRGYKGLITN 

        70         80         90        100        110        120 
EIEDFKTQSV SNIIQRGGTI LKTARCAEFQ TSEGRKLAYD VILQHGINAM IVIGGDGSLR 

       130        140        150        160        170        180 
GARDFAQEYD FPIIGLPGTI DNDLNGTDTT IGYDTALNTI MECVDKIRDT ASSHERLFFV 

       190        200        210        220        230        240 
EVMGRDAGFL ALNGAIASGA EAAIIPEISL KKDQLAEMIE MGFRKSKNSS IVLVAESEVT 

       250        260        270        280        290        300 
GGAMGVAERV KKQYPGFDVR VSILGHLQRG GSPTAQDRIL STRMGVAAVD ALIEGQRNAM 

       310        320        330 
VGIQNEELTL VPFVKAIKKD KPINRDLLNV LRIVST 

« Hide

References

[1]"Complete sequence of Tannerella forsythia ATCC 43037."
Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J., Shetty J., Torralba M., Gill S., Nelson K.
Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43037 / JCM 10827 / FDC 338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003191 Genomic DNA. Translation: AEW22384.1.
RefSeqYP_005014063.1. NC_016610.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW22384; AEW22384; BFO_1157.
GeneID11658166.
KEGGtfo:BFO_1157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

BioCycTFOR203275:GHRQ-1155-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 nameG8UIG9_TANFA
AccessionPrimary (citable) accession number: G8UIG9
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)