6-phosphofructokinase isozyme 1 - Escherichia coli (strain K12)

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P0A796 (K6PF1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
6-phosphofructokinase isozyme 1
EC=2.7.1.11

Alternative name(s):
6-phosphofructokinase isozyme I
Phosphofructokinase 1
Phosphohexokinase 1

Gene names

Name:	pfkA
Ordered Locus Names:	b3916, JW3887

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339
Enzyme regulation	Subject to allosteric activation by ADP and other diphosphonucleosides, and inhibition by phosphoenolpyruvate. 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
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm HAMAP-Rule 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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular carbohydrate catabolic process Inferred from mutant phenotype PubMed 4299078. Source: EcoliWiki fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from direct assay PubMed 15237399. Source: EcoliWiki
Cellular_component	6-phosphofructokinase complex Inferred from direct assay PubMed 6232272. Source: EcoliWiki
Molecular_function	6-phosphofructokinase activity Inferred from direct assay PubMed 4229913. Source: EcoCyc ATP binding Inferred from mutant phenotype PubMed 8202475. Source: EcoliWiki GDP binding Inferred from direct assay PubMed 70226. Source: EcoCyc identical protein binding Inferred from direct assay PubMed 11946283. Source: EcoliWiki magnesium ion binding Inferred from direct assay PubMed 1445885. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 320

320

6-phosphofructokinase isozyme 1 HAMAP-Rule MF_00339

PRO_0000111950

Regions

Nucleotide binding

22 – 26

ATP HAMAP-Rule MF_00339

Nucleotide binding

155 – 159

ATP HAMAP-Rule MF_00339

Nucleotide binding

172 – 188

ATP HAMAP-Rule MF_00339

Sites

Active site

128

Proton acceptor

Metal binding

186

Magnesium; via carbonyl oxygen

Metal binding

188

Magnesium

Binding site

163

Substrate

Binding site

244

Substrate

Binding site

250

Substrate

Binding site

253

Substrate

Experimental info

Mutagenesis

128

D → S: 18000-fold reduction of catalytic rate.

Mutagenesis

172

R → S: 3.4-fold reduction in turnover numbers.

Sequence conflict

F → C in CAA26356. Ref.1

Sequence conflict

103 – 104

GD → DG in CAA26356. Ref.1

Sequence conflict

163

R → P in CAA26356. Ref.1

Sequence conflict

317 – 319

KKL → EKM in CAA26356. Ref.1

Secondary structure

320

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A796 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: D03D79F6A5536A41
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FASTA

320

34,842

        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC 

       130        140        150        160        170        180 
IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA 

       190        200        210        220        230        240 
AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG 

       250        260        270        280        290        300 
RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA 

       310        320 
IENMKRPFKG DWLDCAKKLY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase." Hellinga H.W., Evans P.R. Eur. J. Biochem. 149:363-373(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Mutations in the active site of Escherichia coli phosphofructokinase." Hellinga H.W., Evans P.R. Nature 327:437-439(1987) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION, MUTAGENESIS.
[3]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"A role of RnlA in the RNase LS activity from Escherichia coli." Otsuka Y., Koga M., Iwamoto A., Yonesaki T. Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8. Strain: K12.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[8]	"Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products." Shirakihara Y., Evans P.R. J. Mol. Biol. 204:973-994(1988) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02519 Genomic DNA. Translation: CAA26356.1.
L19201 Genomic DNA. Translation: AAB03048.1.
U00096 Genomic DNA. Translation: AAC76898.1.
AP009048 Genomic DNA. Translation: BAE77394.1.

PIR

KIECFA. G65197.

RefSeq

NP_418351.1. NC_000913.2.
YP_491535.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PFK	X-ray	2.40	A/B	1-320	[»]
2PFK	X-ray	2.40	A/B/C/D	1-320	[»]

ProteinModelPortal

P0A796.

SMR

P0A796. Positions 1-320.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35841N.

IntAct

P0A796. 7 interactions.

MINT

MINT-1322275.

STRING

511145.b3916.

2D gel databases

SWISS-2DPAGE

P0A796.

Proteomic databases

PaxDb

P0A796.

PRIDE

P0A796.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76898; AAC76898; b3916.
BAE77394; BAE77394; BAE77394.

GeneID

12932230.
948412.

KEGG

ecj:Y75_p3271.
eco:b3916.

PATRIC

32123343. VBIEscCol129921_4032.

Organism-specific databases

EchoBASE

EB0693.

EcoGene

EG10699. pfkA.

Phylogenomic databases

eggNOG

COG0205.

HOGENOM

HOG000248870.

K00850.

OMA

EFKTVEG.

ProtClustDB

PRK03202.

Enzyme and pathway databases

BioCyc

EcoCyc:6PFK-1-MONOMER.
ECOL316407:JW3887-MONOMER.
MetaCyc:6PFK-1-MONOMER.

SABIO-RK

P0A796.

UniPathway

UPA00109; UER00182.

Gene expression databases

Genevestigator

P0A796.

Family and domain databases

HAMAP

MF_00339. Phosphofructokinase.

InterPro

IPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]

Pfam

PF00365. PFK. 1 hit.
[Graphical view]

PIRSF

PIRSF000532. ATP_PFK_prok. 1 hit.

PRINTS

PR00476. PHFRCTKINASE.

SUPFAM

SSF53784. Ppfruckinase. 1 hit.

TIGRFAMs

TIGR02482. PFKA_ATP. 1 hit.

PROSITE

PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A796.

Entry information

Entry name

K6PF1_ECOLI

Accession

Primary (citable) accession number: P0A796
Secondary accession number(s): P06998, Q2M8L2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents