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D7CP25 (D7CP25_SYNLT) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 26. 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
Ordered Locus Names:Slip_1702 EMBL ADI02460.1
OrganismSyntrophothermus lipocalidus (strain DSM 12680 / TGB-C1) [Complete proteome] [HAMAP] EMBL ADI02460.1
Taxonomic identifier643648 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesSyntrophomonadaceaeSyntrophothermus

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. SAAS SAAS022953 HAMAP-Rule MF_00339

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
Region213 – 2153Allosteric 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 site2111Allosteric activator ADP 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
D7CP25 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: F2891275BA87B060

FASTA31934,048
        10         20         30         40         50         60 
MKKIAILTSG GDAPGMNAAV RAVVRAGIYA GYQVFGVTRG FQGLINGDFV EMTLGSVADI 

        70         80         90        100        110        120 
IHRGGTILRT SRCEEFMEEK GRLRGLEALR DAGIQDVIGI GGNGTIRGLY EFSKLGVNTV 

       130        140        150        160        170        180 
AIPGSIDNDI PYCDMSIGFD TAVNTVVSAI NRIRDTATAH ERIFIVEVMG RESGHIALTA 

       190        200        210        220        230        240 
GLAGGAESIL IPEVPFDLDQ VVERLKQGMK RGKLHSIIVV AEGCCGAYPL AREIQAKTGM 

       250        260        270        280        290        300 
DTKVTVLGHT QRGGMPSAMD RNLASRMGKR AVDLIVEGKG NMMTGYQGMK IVDVPLAQVI 

       310 
EGKKDIDLDI CEIARILSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002048 Genomic DNA. Translation: ADI02460.1.
RefSeqYP_003703025.1. NC_014220.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADI02460; ADI02460; Slip_1702.
GeneID9274508.
KEGGslp:Slip_1702.
PATRIC38269916. VBISynLip21176_1762.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAAKLERGH.

Enzyme and pathway databases

BioCycSLIP643648:GHUR-1741-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 nameD7CP25_SYNLT
AccessionPrimary (citable) accession number: D7CP25
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: July 9, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)