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 P79273

Entry ID Method Resolution Chain Position Source
AF-P79273-F1 Predicted AlphaFoldDB

No variants for P79273

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P79273

No associated diseases with P79273

5 regional properties for P79273

Type Name Position InterPro Accession
conserved_site Acyl-CoA dehydrogenase, conserved site 153 - 165 IPR006089-1
conserved_site Acyl-CoA dehydrogenase, conserved site 366 - 385 IPR006089-2
domain Acyl-CoA oxidase/dehydrogenase, middle domain 151 - 246 IPR006091
domain Acyl-CoA dehydrogenase/oxidase C-terminal 258 - 407 IPR009075
domain Acyl-CoA dehydrogenase/oxidase, N-terminal 36 - 147 IPR013786

Functions

Description
EC Number 1.3.8.1 With a flavin as acceptor
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
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.

3 GO annotations of molecular function

Name Definition
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
butyryl-CoA dehydrogenase activity Catalysis of the reaction: butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.
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.

2 GO annotations of biological process

Name Definition
butyrate catabolic process The chemical reactions and pathways resulting in the breakdown of butyrate, the anion of butyric acid.
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).

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3ZBF6 ACADS Short-chain specific acyl-CoA dehydrogenase, mitochondrial Bos taurus (Bovine) PR
P16219 ACADS Short-chain specific acyl-CoA dehydrogenase, mitochondrial Homo sapiens (Human) PR
Q9DBL1 Acadsb Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
Q07417 Acads Short-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
MAAALLARAC GPVRGALWPR DCRRLHTIFQ SVELPETYQM LRQTCRDFAE KELVPIAAQV
70 80 90 100 110 120
DKEHRFPEAQ VKKMGELGLM AMDVPEELSG AGLDYLAYTI AMEEISRGCA STGVIMSVNN
130 140 150 160 170 180
FLYLGPILKF GSKEQKQQWI TPFTSGDKVG CFALSEPGNG SDAGAAATTA QADHDSWVLS
190 200 210 220 230 240
GTKAWITNAW EASAAVVFAS TDRSLQNKGI SAFLVPMPTA GLTLGKKEDK LGIRASSTAN
250 260 270 280 290 300
LIFEDCRIPK ENLLGEPGMG FKIAMKTLDM GRIGIASKAL GISQAALDCA VNYAENRRAF
310 320 330 340 350 360
GVPLTKLQGI QFKLADMALA LESARLLTWR AAMLKDNKKN PFIKEPAMAK LAASEAATAI
370 380 390 400 410
THQAIQILGG MGYVTEMPAE RHYRDARITE IYEGTSEIQR LVIAGHLLKS YRS