Q07417

PR
Gene name
Acads
Protein name
Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Names
SCAD, Butyryl-CoA dehydrogenase
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:11409
EC number
1.3.8.1: With a flavin as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

180-261 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q07417

Entry ID Method Resolution Chain Position Source
AF-Q07417-F1 Predicted AlphaFoldDB

13 variants for Q07417

Variant ID(s) Position Change Description Diseaes Association Provenance
rs225839804 89 S>R No EVA
rs3388789549 90 G>S No EVA
rs33137118 94 D>G No EVA
rs3388784246 97 A>V No EVA
rs3388780184 152 F>Y No EVA
rs3388783836 231 L>P No EVA
rs3388776407 260 G>D No EVA
rs3388772091 275 I>F No EVA
rs3388786252 283 A>T No EVA
rs3388772131 284 Q>L No EVA
rs3388755474 287 L>P No EVA
rs3388764439 290 A>V No EVA
rs3388769498 366 I>N No EVA

No associated diseases with Q07417

5 regional properties for Q07417

Type Name Position InterPro Accession
conserved_site Acyl-CoA dehydrogenase, conserved site 153 - 165 IPR006089-1
conserved_site Acyl-CoA dehydrogenase, conserved site 365 - 384 IPR006089-2
domain Acyl-CoA oxidase/dehydrogenase, middle domain 151 - 246 IPR006091
domain Acyl-CoA dehydrogenase/oxidase C-terminal 258 - 406 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

5 GO annotations of cellular component

Name Definition
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
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.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
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.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

5 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.
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.

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).

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
Q9DBL1 Acadsb Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
P50544 Acadvl Very long-chain specific acyl-CoA dehydrogenase, mitochondrial Mus musculus (Mouse) PR
P79273 ACADS Short-chain specific acyl-CoA dehydrogenase, mitochondrial Sus scrofa (Pig) 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
MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL
70 80 90 100 110 120
DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRACA STGVIMSVNN
130 140 150 160 170 180
SLYLGPILKF GSAQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN
190 200 210 220 230 240
GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN
250 260 270 280 290 300
LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF
310 320 330 340 350 360
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS
370 380 390 400 410
HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS