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 P90521

Entry ID Method Resolution Chain Position Source
AF-P90521-F1 Predicted AlphaFoldDB

No variants for P90521

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P90521

No associated diseases with P90521

4 regional properties for P90521

Type Name Position InterPro Accession
domain Phosphofructokinase domain 54 - 356 IPR000023-1
domain Phosphofructokinase domain 439 - 720 IPR000023-2
conserved_site Phosphofructokinase, conserved site 326 - 344 IPR015912-1
conserved_site Phosphofructokinase, conserved site 692 - 710 IPR015912-2

Functions

Description
EC Number 2.7.1.11 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
6-phosphofructokinase complex A protein complex that possesses 6-phosphofructokinase activity; homodimeric, homooctameric, and allosteric homotetrameric forms are known.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

8 GO annotations of molecular function

Name Definition
6-phosphofructokinase activity Catalysis of the reaction: ATP + D-fructose-6-phosphate = ADP + D-fructose 1,6-bisphosphate.
AMP binding Binding to AMP, adenosine monophosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
fructose-6-phosphate binding Binding to fructose 6-phosphate.
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
monosaccharide binding Binding to a monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones HnC(=O)
tubulin binding Binding to monomeric or multimeric forms of tubulin, including microtubules.

5 GO annotations of biological process

Name Definition
canonical glycolysis The glycolytic process that begins with the conversion of glucose to glucose-6-phosphate by glucokinase activity. Glycolytic processes are the chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP.
fructose 1,6-bisphosphate metabolic process The chemical reactions and pathways involving fructose 1,6-bisphosphate, also known as FBP. The D enantiomer is a metabolic intermediate in glycolysis and gluconeogenesis.
fructose 6-phosphate metabolic process The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism.
glucose catabolic process The chemical reactions and pathways resulting in the breakdown of glucose, the aldohexose gluco-hexose.
negative regulation of microtubule polymerization Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTTSKIIND GEGEDVKGNK NINKKSLIDE NRLDEKKDLL SDKVESKTHC SVKRMAVLTS
70 80 90 100 110 120
GGDSSGMNPA IRAFARQVML KGAKVFAVRE GYNGLVNDSI VPLNWGSVAG IISRGGTIIG
130 140 150 160 170 180
TARSAEFRTR EGRKRAVFNL VKNRIDNLLV IGGDGSLTGA NLLRTEWCSL LEELVKDGKL
190 200 210 220 230 240
TLDVMEHFPI LSIAGIVGSI DNDMCGTDLT VGADTATKRI LEAIDSILST AVSHQRSFVI
250 260 270 280 290 300
EVMGRNCGWL ALASGVATGA DYILIPESPP DDGWEQTMAD NLERGRLSGR RCSLVIVSEG
310 320 330 340 350 360
AIDRQGKPIT SAYVRQFLED KGHDARITIL GHVQRGGTPT FLDRYIATRM GIEAANYFYD
370 380 390 400 410 420
STIEQLKQPV LIGMSGMDTI RSPLMECVQK TQSIASLIKE RRFNEVVDVR GGMFKEFYEI
430 440 450 460 470 480
FIACSNLHRR KVESKGMGVL ILHSGGPSPG MNPCVRAFTR LGIDHGYTMY GCFNGFGGLA
490 500 510 520 530 540
LGEIEQLHWM TVNGWSVMGG AELGTNRSIP NDSNIEAIIA TLERFKINAI LMFGGFNGYL
550 560 570 580 590 600
GIAKLYEYRE KYQQLKRISI IGAPGTIANN VPGTNISIGS DTSLNNTLDA LDKIKQSAVA
610 620 630 640 650 660
SRRLFVVEVM GAHCGYLAAM SSLTSGAERS YIMERGITLN TLTKDLEMFV ERFKREHRIG
670 680 690 700 710 720
LIIKSELASN TYSTHFIYSL FKEEGKHLFD VRESILGHLQ QGGTPSAIDR IFSTRLMNHY
730 740 750 760 770 780
YQFLENDLKE HGHLQMNGCI GFIDGGIHYT PMQEMIEEMS DKFRRPRSQW WMDLVETSQN
790 800 810 820 830
ISVFPLDDPS STNFEGCNSN LSEQDRPIKK SDISSPTSYS QKTFDPNVNP QFTL