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Protein

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADSB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciZFISH:HS10828-MONOMER.
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

HGNCiHGNC:91. ACADSB.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: HPA
Complete GO annotation...

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 rs137852649dbSNPEnsembl.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.

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. 14 interactors.
IntActiP45954. 7 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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JIFX-ray2.00A/B/C/D52-432[»]
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.
OMAiGQTTSKC.
OrthoDBiEOG091G04BS.
PhylomeDBiP45954.
TreeFamiTF105055.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

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 → K.2 PublicationsCorresponds to variant rs12263012dbSNPEnsembl.1
Natural variantiVAR_014749209S → G.Corresponds to variant rs1799823dbSNPEnsembl.1
Natural variantiVAR_013010255L → F in SBCADD. 2 PublicationsCorresponds to variant rs137852649dbSNPEnsembl.1
Natural variantiVAR_048178316I → V.1 PublicationCorresponds to variant rs1131430dbSNPEnsembl.1
Natural variantiVAR_048179376E → G.Corresponds to variant rs12357783dbSNPEnsembl.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.
AL731666, AC012391, AC073585 Genomic DNA. Translation: CAI10847.1.
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.
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

Cross-referencesi

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.
AL731666, AC012391, AC073585 Genomic DNA. Translation: CAI10847.1.
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.
NP_001600.1. NM_001609.3. [P45954-1]
UniGeneiHs.81934.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JIFX-ray2.00A/B/C/D52-432[»]
ProteinModelPortaliP45954.
SMRiP45954.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106554. 14 interactors.
IntActiP45954. 7 interactors.
STRINGi9606.ENSP00000357873.

Chemistry databases

DrugBankiDB00167. L-Isoleucine.
DB00313. Valproic Acid.
SwissLipidsiSLP:000001415.

PTM databases

iPTMnetiP45954.
PhosphoSitePlusiP45954.
SwissPalmiP45954.

Polymorphism and mutation databases

BioMutaiACADSB.
DMDMi1168283.

Proteomic databases

EPDiP45954.
PaxDbiP45954.
PeptideAtlasiP45954.
PRIDEiP45954.

Protocols and materials databases

DNASUi36.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi36.
DisGeNETi36.
GeneCardsiACADSB.
HGNCiHGNC:91. ACADSB.
HPAiHPA041458.
MalaCardsiACADSB.
MIMi600301. gene.
610006. phenotype.
neXtProtiNX_P45954.
OpenTargetsiENSG00000196177.
Orphaneti79157. 2-methylbutyryl-CoA dehydrogenase deficiency.
PharmGKBiPA24427.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00660.
BioCyciZFISH:HS10828-MONOMER.
ReactomeiR-HSA-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiACADSB. human.
EvolutionaryTraceiP45954.
GenomeRNAii36.
PROiP45954.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196177.
CleanExiHS_ACADSB.
ExpressionAtlasiP45954. baseline and differential.
GenevisibleiP45954. HS.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACDSB_HUMAN
AccessioniPrimary (citable) accession number: P45954
Secondary accession number(s): B4DQ51, Q5SQN6, Q96CX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 178 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.