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D7AL48 (D7AL48_GEOSK) 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:pfk-2 EMBL ADI84902.1
Synonyms:pfkA HAMAP-Rule MF_00339
Ordered Locus Names:KN400_2090 EMBL ADI84902.1
OrganismGeobacter sulfurreducens (strain DL-1 / KN400) [Complete proteome] [HAMAP] EMBL ADI84902.1
Taxonomic identifier663917 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length319 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
Region125 – 1273Substrate binding By similarity HAMAP-Rule MF_00339
Region169 – 1713Substrate binding By similarity HAMAP-Rule MF_00339
Region185 – 1873Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region249 – 2524Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1271Proton 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 site1541Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1621Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2221Substrate By similarity HAMAP-Rule MF_00339
Binding site2431Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
D7AL48 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 92C4F19B593FD636

FASTA31933,753
        10         20         30         40         50         60 
MKKIGILTSG GDCSGMNAAI RAAVRTAIRM NIEVVGFRKG YLGLMKGDAI PLDTKAVSGI 

        70         80         90        100        110        120 
LHRGGTFLQS ARSPEFKTPE GQRTALNNLK ALGVEGMVVM GGDGSLTGAL ALNRLGLPVV 

       130        140        150        160        170        180 
GIPASIDNDI PFTDMALGVD TALNNIIYAV DCIKDTASSH ARAFVIEVMG RHSGYLASIS 

       190        200        210        220        230        240 
AIATGAEYAL VPEREYDLAE ICQQLRARYE EGRDNAIIIL AEGAGHGHEI ANSIKDAIGF 

       250        260        270        280        290        300 
ETRVTVLGHY QRGGAPTVFD RLLASRLGKK SVELLVTGTW GVMVGLSCNA ILATPLEDVI 

       310 
KGEKRPQDEV LRLAEVLGV 

« Hide

References

[1]"De Novo assembly of the complete genome of an enhanced electricity-producing variant of Geobacter sulfurreducens using only short reads."
Nagarajan H., Butler J.E., Klimes A., Qiu Y., Zengler K., Ward J., Young N.D., Methe B.A., Palsson B.O., Lovley D.R., Barrett C.L.
PLoS ONE 5:E10922-E10922(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DL-1 / KN400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002031 Genomic DNA. Translation: ADI84902.1.
RefSeqYP_006891055.1. NC_017454.1.

3D structure databases

ProteinModelPortalD7AL48.
SMRD7AL48. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADI84902; ADI84902; KN400_2090.
GeneID12440081.
KEGGgsk:KN400_2090.
PATRIC43028244. VBIGeoSul143269_2090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.

Enzyme and pathway databases

BioCycGSUL663917:GLDN-2052-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 nameD7AL48_GEOSK
AccessionPrimary (citable) accession number: D7AL48
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)