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 Q9SVU0

Entry ID Method Resolution Chain Position Source
AF-Q9SVU0-F1 Predicted AlphaFoldDB

18 variants for Q9SVU0

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH02936244 14 L>F No 1000Genomes
ENSVATH02936243 14 L>S No 1000Genomes
tmp_4_14192911_A_G 75 K>R No 1000Genomes
ENSVATH06792834 117 E>D No 1000Genomes
tmp_4_14193040_G_A 118 C>Y No 1000Genomes
ENSVATH12282262 183 D>E No 1000Genomes
ENSVATH12282263 188 E>D No 1000Genomes
tmp_4_14193285_T_A 200 C>S No 1000Genomes
tmp_4_14193337_A_C 217 K>T No 1000Genomes
ENSVATH06792839 241 L>I No 1000Genomes
ENSVATH06792840 249 F>L No 1000Genomes
tmp_4_14193456_A_G 257 I>V No 1000Genomes
ENSVATH06792841 303 R>W No 1000Genomes
tmp_4_14193601_G_A 305 G>E No 1000Genomes
tmp_4_14193678_G_A 331 V>I No 1000Genomes
ENSVATH06792842 346 Y>F No 1000Genomes
ENSVATH14307477 367 N>D No 1000Genomes
tmp_4_14193879_G_A 398 D>N No 1000Genomes

No associated diseases with Q9SVU0

No regional properties for Q9SVU0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9SVU0

Functions

Description
EC Number 1.14.13.168 With NADH or NADPH as one donor, and incorporation of one atom of oxygen
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
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.
indole-3-pyruvate monooxygenase activity Catalysis of the reaction: 3-(indol-3-yl)pyruvate + NADPH + O2 + H+ <=> indole-3-acetate + carbon dioxide + NADP + H2O.
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.

5 GO annotations of biological process

Name Definition
auxin biosynthetic process The chemical reactions and pathways resulting in the formation of auxins, plant hormones that regulate aspects of plant growth.
brassinosteroid mediated signaling pathway The series of molecular signals mediated by the detection of brassinosteroid.
regulation of auxin biosynthetic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of auxins, plant hormones that regulate aspects of plant growth.
response to cytokinin Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cytokinin stimulus.
response to ethylene Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethylene (ethene) stimulus.

13 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38866 FMO1 Thiol-specific monooxygenase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P49326 FMO5 Flavin-containing monooxygenase 5 Homo sapiens (Human) PR
P31512 FMO4 Dimethylaniline monooxygenase [N-oxide-forming] 4 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
P97872 Fmo5 Flavin-containing monooxygenase 5 Mus musculus (Mouse) PR
Q8VHG0 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Mus musculus (Mouse) 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
Q9EQ76 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Rattus norvegicus (Rat) PR
Q8K4C0 Fmo5 Flavin-containing monooxygenase 5 Rattus norvegicus (Rat) 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
MENMFRLMDQ DQDLTNNRCI WVNGPVIVGA GPSGLATAAC LHEQNVPFVV LERADCIASL
70 80 90 100 110 120
WQKRTYDRLK LHLPKQFCQL PKMPFPEDFP EYPTKRQFID YLESYATRFE INPKFNECVQ
130 140 150 160 170 180
TARFDETSGL WRVKTVSKSE STQTEVEYIC RWLVVATGEN AERVMPEIDG LSEFSGEVIH
190 200 210 220 230 240
ACDYKSGEKF AGKKVLVVGC GNSGMEVSLD LANHFAKPSM VVRSSLHVMP REVMGKSTFE
250 260 270 280 290 300
LAMKMLRWFP LWLVDKILLV LSWMVLGNIE KYGLKRPEMG PMELKSVKGK TPVLDIGAIE
310 320 330 340 350 360
KIRLGKINVV PGIKRFNGNK VELVNGEQLD VDSVVLATGY RSNVPYWLQE NEFFAKNGFP
370 380 390 400 410 420
KTVADNNGWK GRTGLYAVGF TRKGLSGASM DAVKIAQDIG SVWQLETKQP TKRSRGSLRR
CISQQF