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 Q04799

Entry ID Method Resolution Chain Position Source
AF-Q04799-F1 Predicted AlphaFoldDB

No variants for Q04799

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q04799

No associated diseases with Q04799

2 regional properties for Q04799

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 1.6.3.1 With oxygen as acceptor
Subcellular Localization
  • Microsome membrane
  • Endoplasmic reticulum membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

6 GO annotations of molecular function

Name Definition
aldehyde oxidase activity Catalysis of the reaction: an aldehyde + H2O + O2 = a carboxylic acid + hydrogen peroxide.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
N,N-dimethylaniline monooxygenase activity Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
NADPH oxidase H202-forming activity Catalysis of the reaction: NADPH + H+ + O2 = NADP + hydrogen peroxide (H2O2).

4 GO annotations of biological process

Name Definition
lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
NADPH oxidation A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADPH, to the oxidized form, NADP.
regulation of cholesterol metabolic process Any process that modulates the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
xenobiotic metabolic process The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAGKRVAVIG AGASGLACIK CCLEEGLEPV CFERTDDIGG LWRFQESPDE GRASIYKSVI
70 80 90 100 110 120
INTSKEMMCF SDYPIPDHFP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKRPDF
130 140 150 160 170 180
STSGQWEVLT ECEGKKESAV FDGVLVCTGH HTSAHLPLES FPGIEKFKGQ YLHSRDYKNP
190 200 210 220 230 240
EKFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW IMNRVGDHGY PIDILLSSRF
250 260 270 280 290 300
SQFLKKITGE TIANSFLERK MNQRFDHAMF GLKPKHRALS QHPTVNDDLP NRIISGSVKI
310 320 330 340 350 360
KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFSFPFLE DSVKVVKNKV SLYKKVFPPN
370 380 390 400 410 420
LEKPTLAIIG LIQPLGAIMP ISELQARWAT LVFKGLKTLP SQSEMMTEIS QVQEKMAKRY
430 440 450 460 470 480
VESQRHTIQG DYIETMEEIA DLVGVRPNLL SLAFTDPRLA LQLLLGPCTP VHYRLQGRGK
490 500 510 520 530
WDGARKTILT VEDRIRKPLM TRVTESSNSV TSMMTMGKFM LAIAFLAIAV VYF