LipidDB ID

LipidDB-9986-00710

Entry Name

UniProt Accession

P00511;

Theoretical PI

8.48

Molecular Weight

85203.39

Genbank Protein ID

AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1; AAA31441.1;

Genbank Nucleotide ID

M14477; M14456; M14457; M14458; M14459; M14460; M14461; M14462; M14463; M14464; M14465; M14466; M14467; M14468; M14469; M14470; M14471; M14472; M14473; M14474; M14475; M14476;

Protein Name

ATP-dependent 6-phosphofructokinase, muscle type

Protein Synonyms/Alias

ATP-PFK; PFK-M; 2.7.1.11; 6-phosphofructokinase type A; Phosphofructo-1-kinase isozyme A; PFK-A; Phosphohexokinase;

Gene Name

PFKM

Gene Synonyms/Alias

Created Date

21-JUL-1986

Organism

Oryctolagus cuniculus (Rabbit)

NCBI Taxa ID

9986

Reference

[1] Jenkins CM, Yang J, Sims HF, Gross RW. Reversible high affinity inhibition of phosphofructokinase-1 by acyl-CoA: a mechanism integrating glycolytic flux withlipid metabolism. J Biol Chem. 2011 Apr 8;286(14):11937-50. doi:10.1074/jbc.M110.203661. Epub 2011 Jan 23.[PMID:21258134]

Functional Description

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Sequence Annotation

Nucleotide-binding: 88 89 ATP.
Nucleotide-binding: 118 121 ATP.
Region: 2 390 N-terminal catalytic PFK domain 1.
Region: 164 166 Substrate binding.
Region: 208 210 Substrate binding.
Region: 298 301 Substrate binding.
Region: 391 401 Interdomain linker.
Region: 402 780 C-terminal regulatory PFK domain 2.
Region: 528 532 Allosteric activator fructose 2,6-bisphosphate binding.
Region: 573 575 Allosteric activator fructose 2,6-bisphosphate binding.
Region: 661 664 Allosteric activator fructose 2,6-bisphosphate binding.
Active site: 166 166 Proton acceptor.
Metal binding site: 119 119 Magnesium; catalytic.
Binding site: 25 25 ATP; via amide nitrogen.
Binding site: 201 201 Substrate; shared with dimeric partner.
Binding site: 264 264 Substrate.
Binding site: 292 292 Substrate; shared with dimeric partner.
Binding site: 471 471 Allosteric activator fructose 2,6-bisphosphate.
Binding site: 566 566 Allosteric activator fructose 2,6-bisphosphate; shared with dimericpartner.
Binding site: 629 629 Allosteric activator fructose 2,6-bisphosphate.
Binding site: 655 655 Allosteric activator fructose 2,6-bisphosphate; shared with dimericpartner.
Binding site: 735 735 Allosteric activator fructose 2,6-bisphosphate.
Modified residue: 2 2 N-acetylthreonine.
Modified residue: 667 667 Phosphoserine.
Modified residue: 775 775 Phosphoserine; by PKA.

Protein Length

780 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0003872; F:6-phosphofructokinase activity; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0008022; F:protein C-terminus binding; IPI:UniProtKB
GO:0046835; P:carbohydrate phosphorylation; IDA:GOC
GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro
GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway

Interpro

InterPro; IPR009161; 6-phosphofructokinase_euk
InterPro; IPR022953; Phosphofructokinase
InterPro; IPR015912; Phosphofructokinase_CS
InterPro; IPR000023; Phosphofructokinase_dom

Pfam

Pfam; PF00365; PFK;

SMART

PROSITE

PROSITE; PS00433; PHOSPHOFRUCTOKINASE;

PRINTS

PRINTS; PR00476; PHFRCTKINASE;