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 Q9DBL1

Entry ID Method Resolution Chain Position Source
AF-Q9DBL1-F1 Predicted AlphaFoldDB

31 variants for Q9DBL1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388952813 11 M>I No EVA
rs3388937139 15 L>Q No EVA
rs238155827 18 R>S No EVA
rs3398656757 19 F>I No EVA
rs252233738 25 P>S No EVA
rs219592578 31 R>H No EVA
rs3388910052 36 S>P No EVA
rs3388957236 38 P>T No EVA
rs580005539 40 A>T No EVA
rs3388953809 41 L>Q No EVA
rs238790641 42 V>L No EVA
rs248500161 44 L>M No EVA
rs48904489 49 V>L No EVA
rs264511938 51 F>C No EVA
rs232394661 66 Q>K No EVA
rs3388956502 71 F>S No EVA
rs3398787046 76 V>C No EVA
rs3398413542 79 L>V No EVA
rs224317312 82 S>P No EVA
rs864295237 161 T>A No EVA
rs3388957313 185 S>P No EVA
rs252596261 210 H>N No EVA
rs582206219 215 E>D No EVA
rs586833939 245 Q>H No EVA
rs3398666573 245 Q>P No EVA
rs3398413543 269 K>N* No EVA
rs586251464 313 I>V No EVA
rs13461151 315 Y>H No EVA
rs3388956362 370 A>V No EVA
rs3388952812 418 N>I No EVA
rs3388957204 422 N>D No EVA

No associated diseases with Q9DBL1

5 regional properties for Q9DBL1

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
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
P15651 Acads Short-chain specific acyl-CoA dehydrogenase, mitochondrial Rattus norvegicus (Rat) PR
P70584 Acadsb Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MAVSALQLWR MGGLLRRRFP TCLSPWKIPP RVLKSSQPEA LVSLTNNAVA FAPLQTLTDE
70 80 90 100 110 120
EIMMKQTVKK FAQEHVAPLV SSMDENSKME KSVIQGLFQQ GLMGIEVEAQ YGGTEASFFC
130 140 150 160 170 180
SVLVIEELAK VDASVALLCD IQNTIINNLF RKHASEEQKA TYLPKLVTEK LGSFCLSEAG
190 200 210 220 230 240
AGSDSFAMKT RADKSGNYYV LNGSKMWISH AEHAELFLVF ANVDPSSGYR GITCFLVDRD
250 260 270 280 290 300
TEGFQIGKRE NKMGIRASST CQLTFENVKV PETNILGKIG HGYKYAIGSL NEGRIGIAAQ
310 320 330 340 350 360
MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAQVA TQLEATRLLT YNAARLVEAG
370 380 390 400 410 420
RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGASNIQ
430
LNTIAKHIDA EY