Q8K4C0

PR
Gene name
Fmo5
Protein name
Flavin-containing monooxygenase 5
Names
FMO 5, Dimethylaniline monooxygenase [N-oxide-forming] 5, Dimethylaniline oxidase 5, Hepatic flavin-containing monooxygenase 5, NADPH oxidase
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:246248
EC number
1.6.3.1: With oxygen as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

229-307 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8K4C0

Entry ID Method Resolution Chain Position Source
AF-Q8K4C0-F1 Predicted AlphaFoldDB

No variants for Q8K4C0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8K4C0

No associated diseases with Q8K4C0

No regional properties for Q8K4C0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8K4C0

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.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P31512 FMO4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Homo sapiens (Human) PR
P49326 FMO5 Flavin-containing monooxygenase 5 Homo sapiens (Human) PR
P97501 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Mus musculus (Mouse) PR
Q8K2I3 Fmo2 Dimethylaniline monooxygenase [N-oxide-forming] 2 Mus musculus (Mouse) PR
Q8VHG0 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Mus musculus (Mouse) PR
P97872 Fmo5 Flavin-containing monooxygenase 5 Mus musculus (Mouse) PR
Q9EQ76 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Rattus norvegicus (Rat) PR
Q8K4B7 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Rattus norvegicus (Rat) PR
Q6IRI9 Fmo2 Dimethylaniline monooxygenase [N-oxide-forming] 2 Rattus norvegicus (Rat) PR
Q9SVU0 YUC8 Probable indole-3-pyruvate monooxygenase YUCCA8 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SXD9 At1g62580 Flavin-containing monooxygenase FMO GS-OX-like 7 Arabidopsis thaliana (Mouse-ear cress) PR
Q9C8T8 At1g63340 Putative flavin-containing monooxygenase FMO GS-OX-like 10 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAKKRIAVIG SGASGLTCIK CCLEEGLEPV CFERSDDIGG LWRYQENPEK GRASIYKSVI
70 80 90 100 110 120
INTSKEMMCF SDYPIPDHYP NFMHNSQVLE YFRMYAKEFG LLKYIQFKTT VCSVKKQPDF
130 140 150 160 170 180
STSGQWQVVT EHEGKQQVDV FDGVLVCTGH HTDPHLPLDS FPGIEKFKGK YFHSREYKNP
190 200 210 220 230 240
VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKRGY PIDILLSSRI
250 260 270 280 290 300
TNYLSKICGS ALKNRYMEKQ LNQRFDHEMF GLKPKHSALG QHPTINDDLP NRIISGLVKV
310 320 330 340 350 360
KGNVKEFTET AAIFEDGSRE DDIDVVIFAT GYSFAFPFLE DSVKVVQNKV SLYKKVFPPN
370 380 390 400 410 420
LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KTREEMAKRY
430 440 450 460 470 480
VDSQRHTIQG DYIDTMEEIA DLVGVRPNLL SLAFTDPKLA FQLLVGPCTP VQYRLQGPGK
490 500 510 520 530
WAGARKTILT TEDRIRKPLM TRVVERDSSG TSLVTVRVLM LAVTFLAVIL AYF