Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

Enzyme regulationi

Phosphorylation results in inhibition of the kinase activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80Fructose 6-phosphateBy similarity1
Binding sitei104Fructose 6-phosphateBy similarity1
Active sitei130Sequence analysis1
Binding sitei132Fructose 6-phosphateBy similarity1
Binding sitei138Fructose 6-phosphateBy similarity1
Active sitei160Sequence analysis1
Binding sitei174Fructose 6-phosphateBy similarity1
Binding sitei195Fructose 6-phosphateBy similarity1
Binding sitei199Fructose 6-phosphateBy similarity1
Binding sitei257Fructose 2,6-bisphosphateBy similarity1
Sitei257Transition state stabilizerBy similarity1
Active sitei258Tele-phosphohistidine intermediateBy similarity1
Binding sitei264Fructose 2,6-bisphosphateBy similarity1
Sitei264Transition state stabilizerBy similarity1
Binding sitei270Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei327Proton donor/acceptorBy similarity1
Binding sitei338Fructose 2,6-bisphosphateBy similarity1
Binding sitei352Fructose 2,6-bisphosphateBy similarity1
Binding sitei356Fructose 2,6-bisphosphateBy similarity1
Binding sitei367Fructose 2,6-bisphosphateBy similarity1
Sitei392Transition state stabilizerBy similarity1
Binding sitei393Fructose 2,6-bisphosphateBy similarity1
Binding sitei397Fructose 2,6-bisphosphateBy similarity1
Binding sitei429ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi47 – 55ATPBy similarity9
Nucleotide bindingi169 – 174ATPBy similarity6
Nucleotide bindingi349 – 352ATPBy similarity4
Nucleotide bindingi393 – 397ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-GGA-352875. Gluconeogenesis.
R-GGA-352882. Glycolysis.
SABIO-RKQ91348.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Short name:
6PF-2-K/Fru-2,6-P2ase
Short name:
PFK/FBPase
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001799721 – 4706-phosphofructo-2-kinase/fructose-2,6-bisphosphataseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Phosphoserine; by PKABy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ91348.

Expressioni

Tissue specificityi

Liver.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ91348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 2496-phosphofructo-2-kinaseAdd BLAST249
Regioni250 – 469Fructose-2,6-bisphosphataseAdd BLAST220

Sequence similaritiesi

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

HOVERGENiHBG005628.
KOiK19028.
PhylomeDBiQ91348.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91348-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVASGQLT QNPLQKVWVP LSLHRLRRRG STVPQFTNCP TMVILVGLRR
60 70 80 90 100
PGKTYISRKL TRYLNWIGMP TRVFNVGQYR REAVQSYKNY EFFRHDNEEA
110 120 130 140 150
MQIRRQCALA ALQDVRTYLS SEEGQVAVFD ATNTTRERRA LIMQFARENG
160 170 180 190 200
YKVLFVESIC DDPAIIEENI KQVKLSSPDY KGCTPEEAVA DFLQRIECYK
210 220 230 240 250
ATYEPLDEQL DSGLSYIKIF DVGVRYLANR VQGHVQSRTV YYLMNTHVTP
260 270 280 290 300
RAIYLSRHGE SQLNLKGRIG GDAGLSTRGR QYAQALAEFI RSQSIRELKV
310 320 330 340 350
WTSHMKRTIE TAEALGVPYE QWKALNEIDA GVCEEMTYEE IQERYPEEFA
360 370 380 390 400
LRDQDKYRYR YPKGESYEDL VQRLEPVIME LERQENVLVI CHQAVMRCLL
410 420 430 440 450
AYFLDKSSEE LPYLRCPLHT VLKLTPVAYG CEVESIFLNV EAVNTHRERP
460 470
QNVDISRPPA EALVTVPEHY
Length:470
Mass (Da):54,404
Last modified:January 16, 2004 - v2
Checksum:iDCDBFB5D392033F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146428 mRNA. Translation: AAD37721.1.
PIRiJC1470.
RefSeqiNP_001025755.1. NM_001030584.1.
UniGeneiGga.17198.

Genome annotation databases

GeneIDi415906.
KEGGigga:415906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146428 mRNA. Translation: AAD37721.1.
PIRiJC1470.
RefSeqiNP_001025755.1. NM_001030584.1.
UniGeneiGga.17198.

3D structure databases

ProteinModelPortaliQ91348.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ91348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi415906.
KEGGigga:415906.

Organism-specific databases

CTDi5210.

Phylogenomic databases

HOVERGENiHBG005628.
KOiK19028.
PhylomeDBiQ91348.

Enzyme and pathway databases

ReactomeiR-GGA-352875. Gluconeogenesis.
R-GGA-352882. Glycolysis.
SABIO-RKQ91348.

Miscellaneous databases

PROiQ91348.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiF26L_CHICK
AccessioniPrimary (citable) accession number: Q91348
Secondary accession number(s): Q9PWA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 16, 2004
Last modified: October 5, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.