[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(87)90348-9; PubMed=2956156 [NCBI, ExPASy, EBI, Israel, Japan] French B.A., Chang S.H.; "Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene."; Gene 54:65-71(1987).
[2]	PROTEIN SEQUENCE. PubMed=6447595 [NCBI, ExPASy, EBI, Israel, Japan] Kolb E., Hudson P.J., Harris J.I.; "Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus."; Eur. J. Biochem. 108:587-597(1980).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319. PubMed=8436141 [NCBI, ExPASy, EBI, Israel, Japan] Sakai H., Ohta T.; "Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon."; Eur. J. Biochem. 211:851-859(1993).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1038/279500a0; PubMed=156307 [NCBI, ExPASy, EBI, Israel, Japan] Evans P.R., Hudson P.J.; "Structure and control of phosphofructokinase from Bacillus stearothermophilus."; Nature 279:500-504(1979).
[5]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1038/343140a0; PubMed=2136935 [NCBI, ExPASy, EBI, Israel, Japan] Schirmer T., Evans P.R.; "Structural basis of the allosteric behaviour of phosphofructokinase."; Nature 343:140-145(1990).
[6]	X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS). DOI=10.1021/bi0263412; PubMed=12390023 [NCBI, ExPASy, EBI, Israel, Japan] Riley-Lovingshimer M.R., Ronning D.R., Sacchettini J.C., Reinhart G.D.; "Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus."; Biochemistry 41:12967-12974(2002).

Comments

CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
ENZYME REGULATION: By ADP and phosphoenolpyruvate.
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: In the R state the 6-P group of fructose 6-phosphate (F6P) is bound by His-249 from one chain and Arg-162 and Arg-243 from an adjacent chain. In the T state a conformation change moves Arg-162 away from the substrate. Glu-161 takes its place, hence repelling the phosphate of ATP.
MISCELLANEOUS: The beta-phosphate group of ADP is bound by Arg-154 from one chain and Arg-21 and Arg-25 from an adjacent chain.
MISCELLANEOUS: The phosphate group of phosphoenolpyruvate appears to bind in the same place as the beta-phosphate group of ADP.
SIMILARITY: Belongs to the phosphofructokinase family.

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

M15643; AAA22656.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D13095; BAA02405.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A27474; KIBSFF.

3D structure databases

PDB

1MTO; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-319.	[ExPASy / RCSB / EBI]
3PFK; X-ray; 2.40 A; A=1-319.	[ExPASy / RCSB / EBI]
4PFK; X-ray; 2.40 A; A=1-319.	[ExPASy / RCSB / EBI]
6PFK; X-ray; 2.60 A; A/B/C/D=1-319.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MTO; -.
3PFK; -.
4PFK; -.
6PFK; -.

ModBase

P00512.

Ontologies

GO:0003872;	Molecular function: 6-phosphofructokinase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00339; -; 1.
PBIL [Tree]

InterPro

IPR012003; ATP_PFK_prok.
IPR012828; PFKA_ATP.
IPR015912; Phosphofructokinase_CS.
IPR000023; Ppfruckinase.
Graphical view of domain structure.

PANTHER

PTHR13697; Ppfruckinase; 1.

Pfam

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

PIRSF

PIRSF000532; ATP_PFK_prok; 1.

PRINTS

PR00476; PHFRCTKINASE.

ProDom

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

TIGRFAMs

TIGR02482; PFKA_ATP; 1.

PROSITE

PS00433; PHOSPHOFRUCTOKINASE; 1.

Other

P00512; -.

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

Keywords

3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 319`	`319`	`6-phosphofructokinase.`	`PRO_0000111935`
`NP_BIND`	`21 25`	`5`	`ATP.`
`NP_BIND`	`154 158`	`5`	`ATP.`
`NP_BIND`	`171 187`	`17`	`ATP.`
`ACT_SITE`	`127 127`		`Proton acceptor.`
`METAL`	`185 185`		`Magnesium; via carbonyl oxygen.`
`METAL`	`187 187`		`Magnesium.`
`BINDING`	`162 162`		`Substrate.`
`BINDING`	`243 243`		`Substrate.`
`BINDING`	`249 249`		`Substrate.`
`BINDING`	`252 252`		`Substrate.`
`CONFLICT`	`12 12`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`35 37`		`Missing (in Ref. 2; AA sequence).`
`CONFLICT`	`43 43`		`G -> V (in Ref. 2; AA sequence).`
`CONFLICT`	`82 82`		`Q -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`95 95`		`E -> Q (in Ref. 2; AA sequence).`
`CONFLICT`	`225 225`		`G -> L (in Ref. 2; AA sequence).`
`STRAND`	`3 11`	`9`
`HELIX`	`16 29`	`14`
`STRAND`	`33 39`	`7`
`HELIX`	`40 45`	`6`
`STRAND`	`49 52`	`4`
`HELIX`	`54 57`	`4`
`HELIX`	`74 76`	`3`
`HELIX`	`79 91`	`13`
`STRAND`	`96 101`	`6`
`HELIX`	`103 114`	`12`
`STRAND`	`119 124`	`6`
`HELIX`	`139 159`	`21`
`STRAND`	`163 168`	`6`
`HELIX`	`175 184`	`10`
`STRAND`	`187 190`	`4`
`HELIX`	`198 210`	`13`
`STRAND`	`216 221`	`6`
`TURN`	`222 224`	`3`
`HELIX`	`227 238`	`12`
`STRAND`	`242 246`	`5`
`HELIX`	`248 252`	`5`
`HELIX`	`258 276`	`19`
`STRAND`	`281 287`	`7`
`STRAND`	`290 295`	`6`
`HELIX`	`296 300`	`5`
`HELIX`	`308 316`	`9`

Sequence information

Length: 319 AA [This is the length of the unprocessed precursor]

Molecular weight: 34119 Da [This is the MW of the unprocessed precursor]

CRC64: EE968D39BA30712B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRIGVLTSG GDSPGMNAAI RSVVRKAIYH GVEVYGVYHG YAGLIAGNIK KLEVGDVGDI 

        70         80         90        100        110        120 
IHRGGTILYT ARCPEFKTEE GQKKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEHGFPCV 

       130        140        150        160        170        180 
GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWS 

       190        200        210        220        230        240 
GLAGGAETIL IPEADYDMND VIARLKRGHE RGKKHSIIIV AEGVGSGVDF GRQIQEATGF 

       250        260        270        280        290        300 
ETRVTVLGHV QRGGSPTAFD RVLASRLGAR AVELLLEGKG GRCVGIQNNQ LVDHDIAEAL 

       310 
ANKHTIDQRM YALSKELSI

P00512 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