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D7BE75 (D7BE75_MEISD) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 24. 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
Ordered Locus Names:Mesil_3101 EMBL ADH64933.1
OrganismMeiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus) [Complete proteome] [HAMAP] EMBL ADH64933.1
Taxonomic identifier526227 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeMeiothermus

Protein attributes

Sequence length322 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 binding72 – 732ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding102 – 1054ATP By similarity HAMAP-Rule MF_00339
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region126 – 1283Substrate binding By similarity HAMAP-Rule MF_00339
Region170 – 1723Substrate binding By similarity HAMAP-Rule MF_00339
Region186 – 1883Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region252 – 2554Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1281Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1031Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site111ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1551Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2121Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2461Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
D7BE75 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: E8886387AB36AAAD

FASTA32233,533
        10         20         30         40         50         60 
MKRIGVFTSG GDAPGMNAAI RAVVRTGTAH GLEVIGIRRG YAGMIEGDFV PLGPRDVANT 

        70         80         90        100        110        120 
LQRGGTILLT ARSAEFKTPE GRAKAAENLR RAGLDGLVCI GGDGSYRGAL KLLEEHHIPV 

       130        140        150        160        170        180 
VGAPGTIDND LYGTDFTIGF DTAVNTALDA IDRIRDTAAS HERVFFIEVM GRHAGFIALE 

       190        200        210        220        230        240 
VGIAGGAEVI VLPEDPLPAS VCAEVISQSS AKGKRSSIVV VAEGGYEGGA EALARDVKAC 

       250        260        270        280        290        300 
SGIEARVTVL GHIQRGGSPT AIDRVLASRL GAGCVDALLS GASGVAVGEV DGEIRLTPFR 

       310        320 
EAVERRKDIN RKKYELAKVL AL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002042 Genomic DNA. Translation: ADH64933.1.
RefSeqYP_003686441.1. NC_014212.1.

3D structure databases

ProteinModelPortalD7BE75.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH64933; ADH64933; Mesil_3101.
GeneID9252626.
KEGGmsv:Mesil_3101.
PATRIC38195081. VBIMeiSil18825_3170.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248869.
KOK00850.
OMAGIYRGYK.

Enzyme and pathway databases

BioCycMSIL526227:GJ9Q-3152-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 nameD7BE75_MEISD
AccessionPrimary (citable) accession number: D7BE75
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: July 9, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)