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 P97501

Entry ID Method Resolution Chain Position Source
AF-P97501-F1 Predicted AlphaFoldDB

49 variants for P97501

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388512106 17 A>V No EVA
rs3388512991 46 H>R No EVA
rs246719414 60 T>A No EVA
rs3388509838 60 T>N No EVA
rs3388511618 68 C>S No EVA
rs3388509968 72 F>S No EVA
rs50797400 76 D>N No EVA
rs3388512689 77 D>V No EVA
rs3388510594 84 H>Q No EVA
rs3388511542 88 Q>H No EVA
rs3388510629 89 E>D No EVA
rs3388510588 90 Y>H No EVA
rs222873067 111 T>S No EVA
rs36935260 118 N>D No EVA
rs3390909993 124 K>N No EVA
rs3388512462 126 E>K No EVA
rs3388511998 151 I>M No EVA
rs37325482 161 P>S No EVA
rs3388512429 175 D>G No EVA
rs50521266 201 A>S No EVA
rs3388512128 242 F>L No EVA
rs3388508386 246 N>D No EVA
rs3388510281 285 N>D No EVA
rs3388512690 296 M>L No EVA
rs32758001 318 M>V No EVA
rs36964758 321 A>D No EVA
rs3390909043 323 D>A No EVA
rs3388511536 324 C>Y No EVA
rs3390890993 325 V>G No EVA
rs3390890990 328 A>D No EVA
rs3388506758 329 T>I No EVA
rs3390909073 330 G>V No EVA
rs227463171 355 G>D No EVA
rs266242565 356 V>I No EVA
rs3388514359 361 L>P No EVA
rs3388511986 408 D>E No EVA
rs3388510614 408 D>V No EVA
rs3388512419 409 I>S No EVA
rs3388511982 410 D>G* No EVA
rs244712117 411 E>K No EVA
rs3388512147 412 K>N No EVA
rs3388511927 413 M>V No EVA
rs3388511613 421 G>D No EVA
rs3388509911 483 R>W No EVA
rs3388512684 500 R>H No EVA
rs265421007 509 C>S No EVA
rs3388506756 519 L>I No EVA
rs3388509897 520 L>Q No EVA
rs37584253 526 L>I No EVA

No associated diseases with P97501

No regional properties for P97501

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P97501

Functions

Description
EC Number 1.14.13.8 With NADH or NADPH as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Microsome membrane ; Single-pass membrane protein
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.

6 GO annotations of molecular function

Name Definition
amino acid binding Binding to an amino acid, organic acids containing one or more amino substituents.
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.
trimethylamine monooxygenase activity Catalysis of the reaction: N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O.

1 GO annotations of biological process

Name Definition
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
P49326 FMO5 Flavin-containing monooxygenase 5 Homo sapiens (Human) PR
P31512 FMO4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Homo sapiens (Human) PR
P97872 Fmo5 Flavin-containing monooxygenase 5 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
Q8K4B7 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Rattus norvegicus (Rat) PR
Q6IRI9 Fmo2 Dimethylaniline monooxygenase [N-oxide-forming] 2 Rattus norvegicus (Rat) PR
Q8K4C0 Fmo5 Flavin-containing monooxygenase 5 Rattus norvegicus (Rat) PR
Q9EQ76 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 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
MKKKVAIIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHIEEG RASIYQSVFT
70 80 90 100 110 120
NSSKEMMCFP DFPYPDDFPN FMHHSKLQEY ITSFAKEKNL LKYIQFETPV TSINKCPNFS
130 140 150 160 170 180
TTGKWEVTTE KHGKKETAVF DATMICSGHH IFPHVPKDSF PGLNRFKGKC FHSRDYKEPG
190 200 210 220 230 240
IWKGKRVLVI GLGNSGCDIA AELSHVAQKV TISSRSGSWV MSRVWDDGYP WDMVVLTRFQ
250 260 270 280 290 300
TFLKNNLPTA ISDWWYTRQM NARFKHENYG LVPLNRTLRK EPVFNDELPA RILCGMVTIK
310 320 330 340 350 360
PNVKEFTETS AVFEDGTMFE AIDCVIFATG YGYAYPFLDD SIIKSRNNEV TLYKGVFPPQ
370 380 390 400 410 420
LEKPTMAVIG LVQSLGATIP ITDLQARWAA QVIKGTCTLP SVNDMMDDID EKMGEKFKWY
430 440 450 460 470 480
GNSTTIQTDY IVYMDELASF IGAKPNLLWL FLKDPRLAVE VFFGPCSPYQ FRLVGPGKWS
490 500 510 520 530
GARNAILTQW DRSLKPMKTR VVSKVQKSCS HFYSRLLRLL AVPVLLIALF LVLI