Reviewed, UniProtKB/Swiss-Prot P00512 (K6PF_BACST)

Names and origin

Protein names

Recommended name:
    6-phosphofructokinase
      Short name=Phosphofructokinase
    EC=2.7.1.11
Alternative name(s):
    Phosphohexokinase

Gene names

Name:	pfkA
Synonyms:	pfk

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP MF_00339
Enzyme regulation	By ADP and phosphoenolpyruvate. HAMAP MF_00339
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP MF_00339
Subunit structure	Homotetramer. HAMAP MF_00339
Subcellular location	Cytoplasm. HAMAP MF_00339
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. HAMAP MF_00339 The beta-phosphate group of ADP is bound by Arg-154 from one chain and Arg-21 and Arg-25 from an adjacent chain. HAMAP MF_00339 The phosphate group of phosphoenolpyruvate appears to bind in the same place as the beta-phosphate group of ADP. HAMAP MF_00339
Sequence similarities	Belongs to the phosphofructokinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular component	6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro
Molecular function	6-phosphofructokinase activity Inferred from electronic annotation. Source: HAMAP ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 319

319

6-phosphofructokinase HAMAP MF_00339

PRO_0000111935

Regions

Nucleotide binding

21 – 25

5

ATP HAMAP MF_00339

Nucleotide binding

154 – 158

5

ATP HAMAP MF_00339

Nucleotide binding

171 – 187

17

ATP HAMAP MF_00339

Sites

Active site

127

1

Proton acceptor HAMAP MF_00339

Metal binding

185

1

Magnesium; via carbonyl oxygen HAMAP MF_00339

Metal binding

187

1

Magnesium HAMAP MF_00339

Binding site

162

1

Substrate HAMAP MF_00339

Binding site

243

1

Substrate HAMAP MF_00339

Binding site

249

1

Substrate HAMAP MF_00339

Binding site

252

1

Substrate HAMAP MF_00339

Experimental info

Sequence conflict

12

1

D → N AA sequence Ref.2

Sequence conflict

35 – 37

3

Missing AA sequence Ref.2

Sequence conflict

43

1

G → V AA sequence Ref.2

Sequence conflict

82

1

Q → E AA sequence Ref.2

Sequence conflict

95

1

E → Q AA sequence Ref.2

Sequence conflict

225

1

G → L AA sequence Ref.2

Secondary structure

1

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319

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Helix

16 – 29

14

Beta strand

33 – 39

7

Helix

40 – 45

6

Beta strand

49 – 52

4

Helix

54 – 57

4

Helix

74 – 76

3

Helix

79 – 91

13

Beta strand

96 – 101

6

Helix

103 – 114

12

Beta strand

119 – 124

6

Helix

139 – 159

21

Beta strand

163 – 168

6

Helix

175 – 184

10

Beta strand

187 – 190

4

Helix

198 – 210

13

Beta strand

216 – 221

6

Turn

222 – 224

3

Helix

227 – 238

12

Beta strand

242 – 246

5

Helix

248 – 252

5

Helix

258 – 276

19

Beta strand

281 – 287

7

Beta strand

290 – 295

6

Helix

296 – 300

5

Helix

308 – 316

9

Sequences

	Sequence		Length	Mass (Da)
	P00512-1 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: EE968D39BA30712B	FASTA	319	34,119
	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

References

[1]	"Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene." French B.A., Chang S.H. Gene 54:65-71(1987) [PubMed: 2956156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Phosphofructokinase: complete amino-acid sequence of the enzyme from Bacillus stearothermophilus." Kolb E., Hudson P.J., Harris J.I. Eur. J. Biochem. 108:587-597(1980) [PubMed: 6447595] [Abstract] Cited for: PROTEIN SEQUENCE.
[3]	"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." Sakai H., Ohta T. Eur. J. Biochem. 211:851-859(1993) [PubMed: 8436141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-319.
[4]	"Structure and control of phosphofructokinase from Bacillus stearothermophilus." Evans P.R., Hudson P.J. Nature 279:500-504(1979) [PubMed: 156307] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[5]	"Structural basis of the allosteric behaviour of phosphofructokinase." Schirmer T., Evans P.R. Nature 343:140-145(1990) [PubMed: 2136935] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[6]	"Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus." Riley-Lovingshimer M.R., Ronning D.R., Sacchettini J.C., Reinhart G.D. Biochemistry 41:12967-12974(2002) [PubMed: 12390023] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15643 Genomic DNA. Translation: AAA22656.1.
D13095 Genomic DNA. Translation: BAA02405.1.

PIR

KIBSFF. A27474.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MTO	X-ray	3.20	A/B/C/D/E/F/G/H	1-319	[»]
3PFK	X-ray	2.40	A	1-319	[»]
4PFK	X-ray	2.40	A	1-319	[»]
6PFK	X-ray	2.60	A/B/C/D	1-319	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.7.1.11. 266715.

Family and domain databases

HAMAP

MF_00339.
[Tree]

InterPro

IPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR000023. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
[Graphical view]

Pfam

PF00365. PFK. 1 hit.
[Graphical view]

PIRSF

PIRSF000532. ATP_PFK_prok. 1 hit.

PRINTS

PR00476. PHFRCTKINASE.

ProDom

PD000707. Ppfruckinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR02482. PFKA_ATP. 1 hit.

PROSITE

PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

K6PF_BACST

Accession

Primary (citable) accession number: P00512

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 96 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)