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 P9WQG3

Entry ID Method Resolution Chain Position Source
AF-P9WQG3-F1 Predicted AlphaFoldDB

No variants for P9WQG3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WQG3

No associated diseases with P9WQG3

3 regional properties for P9WQG3

Type Name Position InterPro Accession
domain Acyl-CoA oxidase/dehydrogenase, middle domain 124 - 205 IPR006091
domain Acyl-CoA dehydrogenase/oxidase C-terminal 239 - 379 IPR009075
domain Acyl-CoA dehydrogenase/oxidase, N-terminal 9 - 119 IPR013786

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
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.

1 GO annotations of biological process

Name Definition
fatty acid beta-oxidation using acyl-CoA dehydrogenase A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTDTSFIESE ERQALRKAVA SWVANYGHEY YLDKARKHEH TSELWAEAGK LGFLGVNLPE
70 80 90 100 110 120
EYGGGGAGMY ELSLVMEEMA AAGSALLLMV VSPAINGTII AKFGTDDQKK RWLPGIADGS
130 140 150 160 170 180
LTMAFAITEP DAGSNSHKIT TTARRDGSDW IIKGQKVFIS GIDQAQAVLV VGRSEEAKTG
190 200 210 220 230 240
KLRPALFVVP TDAPGFSYTP IEMELVSPER QFQVFLDDVR LPADALVGAE DAAIAQLFAG
250 260 270 280 290 300
LNPERIMGAA SAVGMGRFAL GRAVDYVKTR KVWSTPIGAH QGLAHPLAQC HIEVELAKLM
310 320 330 340 350 360
TQKAATLYDH GDDFGAAEAA NMAKYAAAEA SSRAVDQAVQ SMGGNGLTKE YGVAAMMTSA
370 380
RLARIAPISR EMVLNFVAQT SLGLPRSY