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Protein

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADSB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.

Catalytic activityi

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+.

Cofactori

FAD1 Publication

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei183Substrate; via carbonyl oxygen1
Binding sitei283Substrate1
Binding sitei319FAD; shared with dimeric partner1 Publication1
Binding sitei330FAD; shared with dimeric partner1 Publication1
Active sitei414Proton acceptorBy similarity1
Binding sitei415Substrate; via amide nitrogen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi174 – 183FAD1 Publication10
Nucleotide bindingi207 – 209FAD1 Publication3
Nucleotide bindingi387 – 391FAD; shared with dimeric partner1 Publication5
Nucleotide bindingi416 – 418FAD1 Publication3

GO - Molecular functioni

GO - Biological processi

  • branched-chain amino acid catabolic process Source: Reactome
  • fatty acid metabolic process Source: ProtInc

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-HSA-70895 Branched-chain amino acid catabolism
UniPathwayiUPA00660

Chemistry databases

SwissLipidsiSLP:000001415

Names & Taxonomyi

Protein namesi
Recommended name:
Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.5)
Short name:
SBCAD
Alternative name(s):
2-methyl branched chain acyl-CoA dehydrogenase
Short name:
2-MEBCAD
2-methylbutyryl-coenzyme A dehydrogenase
Short name:
2-methylbutyryl-CoA dehydrogenase
Gene namesi
Name:ACADSB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000196177.12
HGNCiHGNC:91 ACADSB
MIMi600301 gene
neXtProtiNX_P45954

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive disorder and consists of a defect in catabolism of L-isoleucine which is characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine. Affected individuals have seizures and psychomotor delay as the main clinical features.
See also OMIM:610006
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013010255L → F in SBCADD. 2 PublicationsCorresponds to variant dbSNP:rs137852649EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi36
MalaCardsiACADSB
MIMi610006 phenotype
OpenTargetsiENSG00000196177
Orphaneti79157 2-methylbutyryl-CoA dehydrogenase deficiency
PharmGKBiPA24427

Chemistry databases

DrugBankiDB00167 L-Isoleucine
DB00313 Valproic Acid

Polymorphism and mutation databases

BioMutaiACADSB
DMDMi1168283

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33MitochondrionAdd BLAST33
ChainiPRO_000000051934 – 432Short/branched chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST399

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei70N6-acetyllysine; alternateBy similarity1
Modified residuei70N6-succinyllysine; alternateBy similarity1
Modified residuei183PhosphoserineCombined sources1
Modified residuei284N6-acetyllysine; alternateCombined sources1
Modified residuei284N6-succinyllysine; alternateBy similarity1
Modified residuei426N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP45954
PaxDbiP45954
PeptideAtlasiP45954
PRIDEiP45954
ProteomicsDBi55690

PTM databases

iPTMnetiP45954
PhosphoSitePlusiP45954
SwissPalmiP45954

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000196177
CleanExiHS_ACADSB
ExpressionAtlasiP45954 baseline and differential
GenevisibleiP45954 HS

Organism-specific databases

HPAiHPA041458

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi106554, 16 interactors
IntActiP45954, 12 interactors
STRINGi9606.ENSP00000357873

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi59 – 75Combined sources17
Helixi77 – 79Combined sources3
Helixi80 – 86Combined sources7
Helixi91 – 99Combined sources9
Turni100 – 103Combined sources4
Beta strandi104 – 107Combined sources4
Helixi109 – 111Combined sources3
Helixi118 – 129Combined sources12
Helixi133 – 144Combined sources12
Helixi146 – 153Combined sources8
Helixi156 – 168Combined sources13
Beta strandi172 – 175Combined sources4
Beta strandi181 – 184Combined sources4
Helixi185 – 187Combined sources3
Beta strandi191 – 195Combined sources5
Beta strandi198 – 209Combined sources12
Turni210 – 213Combined sources4
Beta strandi215 – 223Combined sources9
Helixi225 – 231Combined sources7
Beta strandi232 – 238Combined sources7
Beta strandi244 – 246Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi260 – 271Combined sources12
Helixi272 – 274Combined sources3
Beta strandi275 – 278Combined sources4
Helixi282 – 318Combined sources37
Helixi326 – 328Combined sources3
Helixi330 – 358Combined sources29
Helixi364 – 389Combined sources26
Helixi390 – 394Combined sources5
Helixi400 – 407Combined sources8
Helixi408 – 411Combined sources4
Turni412 – 414Combined sources3
Helixi417 – 431Combined sources15

3D structure databases

ProteinModelPortaliP45954
SMRiP45954
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45954

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 230Substrate binding2
Regioni291 – 294Substrate binding4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0139 Eukaryota
COG1960 LUCA
GeneTreeiENSGT00760000119007
HOGENOMiHOG000131659
HOVERGENiHBG000224
InParanoidiP45954
KOiK09478
OMAiYKIAIEI
OrthoDBiEOG091G04BS
PhylomeDBiP45954
TreeFamiTF105055

Family and domain databases

Gene3Di1.10.540.10, 1 hit
InterProiView protein in InterPro
IPR006089 Acyl-CoA_DH_CS
IPR006091 Acyl-CoA_Oxase/DH_cen-dom
IPR036250 AcylCo_DH-like_C
IPR009075 AcylCo_DH/oxidase_C
IPR013786 AcylCoA_DH/ox_N
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom
PfamiView protein in Pfam
PF00441 Acyl-CoA_dh_1, 1 hit
PF02770 Acyl-CoA_dh_M, 1 hit
PF02771 Acyl-CoA_dh_N, 1 hit
SUPFAMiSSF47203 SSF47203, 1 hit
SSF56645 SSF56645, 1 hit
PROSITEiView protein in PROSITE
PS00072 ACYL_COA_DH_1, 1 hit
PS00073 ACYL_COA_DH_2, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P45954-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGLAVRLLR GSRLLRRNFL TCLSSWKIPP HVSKSSQSEA LLNITNNGIH
60 70 80 90 100
FAPLQTFTDE EMMIKSSVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ
110 120 130 140 150
GLMGIEVDPE YGGTGASFLS TVLVIEELAK VDASVAVFCE IQNTLINTLI
160 170 180 190 200
RKHGTEEQKA TYLPQLTTEK VGSFCLSEAG AGSDSFALKT RADKEGDYYV
210 220 230 240 250
LNGSKMWISS AEHAGLFLVM ANVDPTIGYK GITSFLVDRD TPGLHIGKPE
260 270 280 290 300
NKLGLRASST CPLTFENVKV PEANILGQIG HGYKYAIGSL NEGRIGIAAQ
310 320 330 340 350
MLGLAQGCFD YTIPYIKERI QFGKRLFDFQ GLQHQVAHVA TQLEAARLLT
360 370 380 390 400
YNAARLLEAG KPFIKEASMA KYYASEIAGQ TTSKCIEWMG GVGYTKDYPV
410 420 430
EKYFRDAKIG TIYEGASNIQ LNTIAKHIDA EY
Length:432
Mass (Da):47,485
Last modified:November 1, 1995 - v1
Checksum:i1EB5F894B1944E99
GO
Isoform 2 (identifier: P45954-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Note: No experimental confirmation available.
Show »
Length:330
Mass (Da):36,025
Checksum:i1BFB4E4C8E0F3615
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04817713R → K2 PublicationsCorresponds to variant dbSNP:rs12263012EnsemblClinVar.1
Natural variantiVAR_014749209S → G. Corresponds to variant dbSNP:rs1799823Ensembl.1
Natural variantiVAR_013010255L → F in SBCADD. 2 PublicationsCorresponds to variant dbSNP:rs137852649EnsemblClinVar.1
Natural variantiVAR_048178316I → V1 PublicationCorresponds to variant dbSNP:rs1131430EnsemblClinVar.1
Natural variantiVAR_048179376E → G. Corresponds to variant dbSNP:rs12357783Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0557781 – 102Missing in isoform 2. 1 PublicationAdd BLAST102

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12778 mRNA Translation: AAA74424.1
AF260678
, AF260668, AF260669, AF260670, AF260671, AF260672, AF260673, AF260674, AF260675, AF260676, AF260677 Genomic DNA Translation: AAF97921.1
AK298638 mRNA Translation: BAG60813.1
AK314241 mRNA Translation: BAG36909.1
AC012391 Genomic DNA No translation available.
AC073585 Genomic DNA No translation available.
AL731666 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49291.1
BC013756 mRNA Translation: AAH13756.1
AL831821 mRNA Translation: CAD38535.2
CCDSiCCDS7634.1 [P45954-1]
CCDS81518.1 [P45954-2]
PIRiA55680
RefSeqiNP_001317103.1, NM_001330174.1 [P45954-2]
NP_001600.1, NM_001609.3 [P45954-1]
UniGeneiHs.81934

Genome annotation databases

EnsembliENST00000358776; ENSP00000357873; ENSG00000196177 [P45954-1]
ENST00000368869; ENSP00000357862; ENSG00000196177 [P45954-2]
GeneIDi36
KEGGihsa:36
UCSCiuc001lhb.4 human [P45954-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiACDSB_HUMAN
AccessioniPrimary (citable) accession number: P45954
Secondary accession number(s): B4DQ51, Q5SQN6, Q96CX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 20, 2018
This is version 189 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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