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 P70584

Entry ID Method Resolution Chain Position Source
AF-P70584-F1 Predicted AlphaFoldDB

No variants for P70584

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P70584

No associated diseases with P70584

5 regional properties for P70584

Type Name Position InterPro Accession
conserved_site Acyl-CoA dehydrogenase, conserved site 175 - 187 IPR006089-1
conserved_site Acyl-CoA dehydrogenase, conserved site 387 - 406 IPR006089-2
domain Acyl-CoA oxidase/dehydrogenase, middle domain 173 - 268 IPR006091
domain Acyl-CoA dehydrogenase/oxidase C-terminal 280 - 428 IPR009075
domain Acyl-CoA dehydrogenase/oxidase, N-terminal 58 - 168 IPR013786

Functions

Description
EC Number 1.3.8.5 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.

7 GO annotations of molecular function

Name Definition
2-methylacyl-CoA dehydrogenase activity Catalysis of the reaction: 2-methylbutanoyl-CoA + H+ + oxidized = (2E)-2-methylbut-2-enoyl-CoA + reduced
acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + oxidized
electron transfer activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
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.
isobutyryl-CoA:FAD oxidoreductase activity Catalysis of the reaction: H+ + isobutyryl-CoA + FAD <=> methacrylyl-CoA + FADH2.
short-branched-chain-acyl-CoA dehydrogenase activity Catalysis of the reaction: acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor, where the acyl group is a short branched chain fatty acid residue.

4 GO annotations of biological process

Name Definition
acyl-CoA metabolic process The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group.
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 metabolic process The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
isoleucine catabolic process The chemical reactions and pathways resulting in the breakdown of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.

7 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
Q07417 Acads Short-chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
Q9DBL1 Acadsb Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
P79273 ACADS Short-chain specific acyl-CoA dehydrogenase, mitochondrial Sus scrofa (Pig) PR
P45953 Acadvl Very long-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
MAVSAFQLWR AGGLLRRNFL THSSSWKIPP RVLKSSQPEA LLSVTNNALC FAPLQTFTDE
70 80 90 100 110 120
DIMMQKAVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ GMMGIEVEAK YGGTEASFLC
130 140 150 160 170 180
SVLVIEELAK VDASVALLCD IQNTVINKLF RKHGTEEQKA TYLPKLVTEK LGSFCLSEAG
190 200 210 220 230 240
AGSDSFALKT RADKSGNYYV INGSKMWISN AEHAELFLVF ANVDPPSGYR GITCFLVDRD
250 260 270 280 290 300
TEGFQIGRRE NKMGIRASST CQLTFENVKV PETSVLGKIG HGYKYAIGSL NEGRIGIAAQ
310 320 330 340 350 360
MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAHVA TQLEAARLLT YNAARLVEAG
370 380 390 400 410 420
RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGTSNIQ
430
LNTIAKHIDA EY