EC 2.7.1.90
6-phosphofructokinase, pyrophosphate dependent
Pyrophosphate-dependent 6-phosphofructose-1-kinase
PPi-dependent phosphofructokinase
PPi-PFK

Gene name

	Name:	pfp
	Synonyms:	pfk

From

Propionibacterium freudenreichii subsp. shermanii

[TaxID: 1752]

Taxonomy

Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Propionibacterineae; Propionibacteriaceae; Propionibacterium.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=1653240 [NCBI, ExPASy, EBI, Israel, Japan] Ladror U.S., Gollapudi L., Tripathi R.L., Latshaw S.P., Kemp R.G.; "Cloning, sequencing, and expression of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii."; J. Biol. Chem. 266:16550-16555(1991).
[2]	IDENTIFICATION OF CRITICAL LYSYL RESIDUES. DOI=10.1021/bi00135a011; PubMed=1317210 [NCBI, ExPASy, EBI, Israel, Japan] Green P.C., Latshaw S.P., Ladror U.S., Kemp R.G.; "Identification of critical lysyl residues in the pyrophosphate-dependent phosphofructo-1-kinase of Propionibacterium freudenreichii."; Biochemistry 31:4815-4821(1992).

Comments

CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate.
ENZYME REGULATION: Non-allosteric.
PATHWAY: Carbohydrate degradation; glycolysis .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the phosphofructokinase family. PFP subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M67447; AAA25675.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41169; A41169.

3D structure databases

ModBase

P29495.

Ontologies

GO:0005945;	Cellular component: 6-phosphofructokinase complex (inferred from electronic annotation from InterPro).
GO:0003872;	Molecular function: 6-phosphofructokinase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0047334;	Molecular function: diphosphate-fructose-6-phosphate 1-phosphotransferase activity (inferred from electronic annotation from EC).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000023; Ppfruckinase.
IPR011405; PPi-PFK_SMc01852.
Graphical view of domain structure.

PANTHER

PTHR13697; Ppfruckinase; 1.

Pfam

PF00365; PFK; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036484; PPi-PFK_SMc01852; 1.

PRINTS

PR00476; PHFRCTKINASE.

ProDom

PD000707; Ppfruckinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 404`	`403`	`Pyrophosphate--fructose 6-phosphate 1-phosphotransferase.`	`PRO_0000112013`
`NP_BIND`	`22 26`	`5`	`ATP (By similarity).`
`NP_BIND`	`121 126`	`6`	`Pyrophosphate (Potential).`
`NP_BIND`	`179 183`	`5`	`ATP (By similarity).`
`NP_BIND`	`196 232`	`37`	`ATP (By similarity).`
`ACT_SITE`	`151 151`		`Proton acceptor (By similarity).`
`BINDING`	`326 326`		`Substrate (By similarity).`

Sequence information

Length: 404 AA [This is the length of the unprocessed precursor]

Molecular weight: 43246 Da [This is the MW of the unprocessed precursor]

CRC64: 2676CD4ADE0D8A55 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKKVALLTA GGFAPCLSSA IAELIKRYTE VSPETTLIGY RYGYEGLLKG DSLEFSPAVR 

        70         80         90        100        110        120 
AHYDRLFSFG GSPIGNSRVK LTNVKDLVAR GLVASGDDPL KVAADQLIAD GVDVLHTIGG 

       130        140        150        160        170        180 
DDTNTTAADL AAYLAQHDYP LTVVGLPKTI DNDIVPIRQS LGAWTAADEG ARFAANVIAE 

       190        200        210        220        230        240 
HNAAPRELII HEIMGRNCGY LAAETSRRYV AWLDAQQWLP EAGLDRRGWD IHALYVPEAT 

       250        260        270        280        290        300 
IDLDAEAERL RTVMDEVGSV NIFISEGAGV PDIVAQMQAT GQEVPTDAFG HVQLDKINPG 

       310        320        330        340        350        360 
AWFAKQFAER IGAGKTMVQK SGYFSRSAKS NAQDLELIAA TATMAVDAAL AGTPGVVGQD 

       370        380        390        400 
EEAGDKLSVI DFKRIAGHKP FDITLDWYTQ LLARIGQPAP IAAA

P29495 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools