Reviewed, UniProtKB/Swiss-Prot P29495 (PFP_PROFR)

Names and origin

Protein names

Recommended name:
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
    EC=2.7.1.90
Alternative name(s):
    6-phosphofructokinase, pyrophosphate dependent
    Pyrophosphate-dependent 6-phosphofructose-1-kinase
    PPi-dependent phosphofructokinase
      Short name=PPi-PFK

Gene names

Name:	pfp
Synonyms:	pfk

Organism

Propionibacterium freudenreichii subsp. shermanii

Taxonomic identifier

1752 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate.
Enzyme regulation	Non-allosteric.
Pathway	Carbohydrate degradation; glycolysis.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the phosphofructokinase family. PFP subfamily.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro
Cellular component	6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro
Molecular function	6-phosphofructokinase activity Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diphosphate-fructose-6-phosphate 1-phosphotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 404	403	Pyrophosphate--fructose 6-phosphate 1-phosphotransferase		PRO_0000112013
Regions
	Nucleotide binding	22 – 26	5	ATP By similarity
	Nucleotide binding	121 – 126	6	Pyrophosphate Potential
	Nucleotide binding	179 – 183	5	ATP By similarity
	Nucleotide binding	196 – 232	37	ATP By similarity
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	326	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29495-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2676CD4ADE0D8A55	FASTA	404	43,246
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	M67447 Genomic DNA. Translation: AAA25675.1.
PIR	A41169.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.90. 4086.
Family and domain databases
InterPro	IPR000023. Phosphofructokinase. IPR011405. PPi-PFK_SMc01852. [Graphical view]
Pfam	PF00365. PFK. 1 hit. [Graphical view]
PIRSF	PIRSF036484. PPi-PFK_SMc01852. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
ProDom	PD000707. Ppfruckinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

PFP_PROFR

Accession

Primary (citable) accession number: P29495

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)