6-phosphofructokinase, liver type - Rattus norvegicus (Rat)

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P30835 (K6PL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. History...

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

Documents (2) |

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, liver type
EC=2.7.1.11

Alternative name(s):
Phosphofructo-1-kinase isozyme B
Short name=PFK-B
Phosphofructokinase 1
Phosphohexokinase

Gene names

Name:	Pfkl
Synonyms:	Pfk-l

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	780 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.
Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
Cofactor	Magnesium.
Enzyme regulation	Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. GlcNAcylation by OGT overcomes allosteric regulation By similarity.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subunit structure	Homotetramer.
Post-translational modification	GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation By similarity.
Sequence similarities	Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fructose 1,6-bisphosphate metabolic process Inferred from direct assay PubMed 2931076 PubMed 4273555. Source: RGD fructose 6-phosphate metabolic process Inferred from direct assay PubMed 14342527 PubMed 156182 PubMed 2931076 PubMed 4273555 PubMed 6240262 PubMed 6446905 PubMed 6458283. Source: RGD glycolysis Inferred from direct assay PubMed 2931076 PubMed 4273555 PubMed 4353083 PubMed 6458283. Source: RGD negative regulation of insulin secretion Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from direct assay PubMed 2931076. Source: RGD response to glucose stimulus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	6-phosphofructokinase complex Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 1834654 PubMed 6240262. Source: RGD
Molecular_function	6-phosphofructokinase activity Inferred from direct assay PubMed 14342527 PubMed 156182 PubMed 1834654 PubMed 2931076 PubMed 4273555 PubMed 6240262 PubMed 6446905 PubMed 6458283. Source: RGD ATP binding Inferred from direct assay PubMed 14342527 PubMed 156182 PubMed 2931076 PubMed 6446905 PubMed 6458283. Source: RGD fructose binding Inferred from electronic annotation. Source: Compara fructose-2,6-bisphosphate 2-phosphatase activity Traceable author statement PubMed 12482582. Source: RGD fructose-6-phosphate binding Inferred from direct assay PubMed 2931076 PubMed 4273555. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW monosaccharide binding Inferred from direct assay PubMed 14342527 PubMed 156182 PubMed 6446905 PubMed 6458283. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 780

779

6-phosphofructokinase, liver type

PRO_0000112023

Regions

Nucleotide binding

35 – 39

ATP By similarity

Nucleotide binding

193 – 197

ATP By similarity

Nucleotide binding

210 – 226

ATP By similarity

Sites

Active site

166

Proton acceptor By similarity

Metal binding

224

Magnesium; via carbonyl oxygen By similarity

Binding site

201

Substrate By similarity

Binding site

292

Substrate By similarity

Binding site

298

Substrate By similarity

Binding site

301

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

640

Phosphotyrosine By similarity

Modified residue

775

Phosphoserine By similarity

Glycosylation

529

O-linked (GlcNAc...) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P30835 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7F6FCFB076D6A0F1
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FASTA

780

85,339

        10         20         30         40         50         60 
MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE 

        70         80         90        100        110        120 
GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA AAYNLLQHGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGANIFRN EWGSLLEELV KEGKISESTA QNYAHLSIAG LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE 

       250        260        270        280        290        300 
NFMCERLGET RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 

       310        320        330        340        350        360 
RGGTPSAFDR VLSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME CVQVTKDVQK 

       370        380        390        400        410        420 
AMDEKRFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF SLAILNVGAP AAGMNAAVRS 

       430        440        450        460        470        480 
AVRTGISEGH TVYVVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI 

       490        500        510        520        530        540 
VENLRTYNIH ALLVIGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG 

       550        560        570        580        590        600 
SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 

       610        620        630        640        650        660 
IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV FDCRTNVLGH 

       670        680        690        700        710        720 
LQQGGAPTPF DRNYGTKLGV KAMLWMSEKL RDVYRKGRVF ANAPDSACVI GLRKKVVAFS 

       730        740        750        760        770        780 
SVTELKKETD FEHRMPREQW WLNLRLMLKM LAHYRISMAD YVSGELEHVT RRTLSIDKGF

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References

[1]	"Rat-liver-type phosphofructokinase mRNA. Structure, tissue distribution and regulation." Hotta K., Nakajima H., Yamasaki T., Hamaguchi T., Kuwajima M., Noguchi T., Tanaka T., Kono N., Tarui S. Eur. J. Biochem. 202:293-298(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58865 mRNA. Translation: CAA41674.1.
IPI	IPI00212741.
PIR	S19689.
RefSeq	NP_037322.1. NM_013190.4.
UniGene	Rn.4212.
3D structure databases
ProteinModelPortal	P30835.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30835. 1 interaction.
STRING	10116.ENSRNOP00000001625.
PTM databases
PhosphoSite	P30835.
Proteomic databases
PaxDb	P30835.
PRIDE	P30835.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000001625; ENSRNOP00000001625; ENSRNOG00000001214.
GeneID	25741.
KEGG	rno:25741.
UCSC	RGD:3311. rat.
Organism-specific databases
CTD	5211.
RGD	3311. Pfkl.
Phylogenomic databases
eggNOG	COG0205.
GeneTree	ENSGT00390000013209.
HOGENOM	HOG000200154.
HOVERGEN	HBG000976.
InParanoid	P30835.
KO	K00850.
OMA	PISSSYV.
OrthoDB	EOG4RJG0W.
Enzyme and pathway databases
SABIO-RK	P30835.
UniPathway	UPA00109; UER00182.
Gene expression databases
Genevestigator	P30835.
GermOnline	ENSRNOG00000001214. Rattus norvegicus.
Family and domain databases
InterPro	IPR009161. 6-phosphofructokinase_euk. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view]
Pfam	PF00365. PFK. 2 hits. [Graphical view]
PIRSF	PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
SUPFAM	SSF53784. Ppfruckinase. 2 hits.
TIGRFAMs	TIGR02478. 6PF1K_euk. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	607897.

Entry information

Entry name

K6PL_RAT

Accession

Primary (citable) accession number: P30835

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM 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