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 P45953

Entry ID Method Resolution Chain Position Source
AF-P45953-F1 Predicted AlphaFoldDB

No variants for P45953

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P45953

No associated diseases with P45953

2 regional properties for P45953

Type Name Position InterPro Accession
binding_site PPM-type phosphatase, divalent cation binding 265 - 273 IPR000222
domain PPM-type phosphatase-like domain 216 - 485 IPR001932

Functions

Description
EC Number 1.3.8.9 With a flavin as acceptor
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
extrinsic component of mitochondrial inner membrane The component of mitochondrial inner membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
mitochondrial nucleoid The region of a mitochondrion to which the DNA is confined.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

6 GO annotations of molecular function

Name Definition
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
fatty-acyl-CoA binding Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group.
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.
identical protein binding Binding to an identical protein or proteins.
long-chain-acyl-CoA dehydrogenase activity Catalysis of the reaction: a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a long-chain (2E)-enoyl-CoA + reduced
very-long-chain-acyl-CoA dehydrogenase activity Catalysis of the reaction: a very-long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a very-long-chain (2E)-enoyl-CoA + reduced

9 GO annotations of biological process

Name Definition
epithelial cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium.
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
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).
fatty acid catabolic process The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
negative regulation of fatty acid biosynthetic process Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids.
negative regulation of fatty acid oxidation Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid oxidation.
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.
response to cold 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 cold stimulus, a temperature stimulus below the optimal temperature for that organism.
temperature homeostasis A homeostatic process in which an organism modulates its internal body temperature.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P48818 ACADVL Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Bos taurus (Bovine) PR
P49748 ACADVL Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Homo sapiens (Human) PR
P50544 Acadvl Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
P70584 Acadsb Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial Rattus norvegicus (Rat) PR
P15651 Acads Short-chain specific acyl-CoA dehydrogenase, mitochondrial Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MQSARMTPSV GRQLLRLGAR SSRSAALQGQ PRPTSAQRLY ASEATQAVLE KPETLSSDAS
70 80 90 100 110 120
TREKPARAES KSFAVGMFKG QLTTDQVFPY PSVLNEGQTQ FLKELVGPVA RFFEEVNDPA
130 140 150 160 170 180
KNDSLEKVEE DTLQGLKELG AFGLQVPSEL GGLGLSNTQY ARLAEIVGMH DLGVSVTLGA
190 200 210 220 230 240
HQSIGFKGIL LYGTKAQKEK YLPRVASGQA LAAFCLTEPS SGSDVASIRS SAVPSPCGKY
250 260 270 280 290 300
YTLNGSKIWI SNGGLADIFT VFAKTPIKDA ATGAVKEKIT AFVVERSFGG VTHGLPEKKM
310 320 330 340 350 360
GIKASNTSEV YFDGVKVPAE NVLGEVGDGF KVAVNILNNG RFGMAATLAG TMKAIIAKAV
370 380 390 400 410 420
DHATNRTQFG DKIHNFGVIQ EKLARMAILQ YVTESMAYML SANMDQGFKD FQIEAAISKI
430 440 450 460 470 480
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDIRIFRI FEGTNDILRL FVALQGCMDK
490 500 510 520 530 540
GKELTGLGNA LKNPLGNVGL LIGEASKQLR RRTGIGSGLS LSGIVHPELS RSGELAVQAL
550 560 570 580 590 600
EQFATVVEAK LMKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGYPTAQHEK
610 620 630 640 650
MLCDSWCIEA ATRIRENMAS LQSNPQQQEL FRNFRSISKA MVENGGLVTS NPLRV