Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P49872

Entry ID Method Resolution Chain Position Source
AF-P49872-F1 Predicted AlphaFoldDB

No variants for P49872

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P49872

No associated diseases with P49872

2 regional properties for P49872

Type Name Position InterPro Accession
active_site Phosphoglycerate/bisphosphoglycerate mutase, active site 256 - 265 IPR001345
domain 6-phosphofructo-2-kinase 31 - 251 IPR013079

Functions

Description
EC Number 2.7.1.105 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex A homodimeric, bifunctional enzyme complex which catalyzes the synthesis and degradation of fructose 2,6-bisphosphate, and is required for both glycolysis and gluconeogenesis.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

3 GO annotations of molecular function

Name Definition
6-phosphofructo-2-kinase activity Catalysis of the reaction: beta-D-fructose 6-phosphate + ATP = beta-D-fructose 2,6-bisphosphate + ADP + 2 H(+).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
fructose-2,6-bisphosphate 2-phosphatase activity Catalysis of the reaction: D-fructose 2,6-bisphosphate + H2O = D-fructose-6-phosphate + phosphate.

2 GO annotations of biological process

Name Definition
fructose 2,6-bisphosphate metabolic process The chemical reactions and pathways involving fructose 2,6-bisphosphate. The D enantiomer is an important regulator of the glycolytic and gluconeogenic pathways. It inhibits fructose 1,6-bisphosphatase and activates phosphofructokinase.
fructose metabolic process The chemical reactions and pathways involving fructose, the ketohexose arabino-2-hexulose. Fructose exists in a open chain form or as a ring compound. D-fructose is the sweetest of the sugars and is found free in a large number of fruits and honey.

13 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32604 FBP26 Fructose-2,6-bisphosphatase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P26285 PFKFB2 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 Bos taurus (Bovine) PR
Q16877 PFKFB4 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 Homo sapiens (Human) PR
O60825 PFKFB2 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 Homo sapiens (Human) PR
Q16875 PFKFB3 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens (Human) PR
P16118 PFKFB1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 Homo sapiens (Human) PR
Q6DTY7 Pfkfb4 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 Mus musculus (Mouse) PR
P70265 Pfkfb2 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 Mus musculus (Mouse) PR
P70266 Pfkfb1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 Mus musculus (Mouse) PR
Q9JJH5 Pfkfb2 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 Rattus norvegicus (Rat) PR
P25114 Pfkfb4 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 Rattus norvegicus (Rat) PR
O35552 Pfkfb3 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Rattus norvegicus (Rat) PR
P07953 Pfkfb1 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSQEMGELTQ TRLQKIWIPH NNGNSRLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST
70 80 90 100 110 120
KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME ALLIRKQCAL AALKDVHSYL
130 140 150 160 170 180
SHEEGRVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPDVIAEN IRQVKLGSPD
190 200 210 220 230 240
YIDCDREKVL EDFLKRIECY EVNYQPLDDE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT
250 260 270 280 290 300
VYYLMNIHVT PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IQSQGISSLK
310 320 330 340 350 360
VGTSHMKRTI QTAEALGLPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY
370 380 390 400 410 420
RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH
430 440 450 460 470
TVLKLTPVAY GCKVESIYLN VEAVNTHREK PENVDITREP EEALDTVPAH Y