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Protein

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadsb

Organism
Rattus norvegicus (Rat)
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.1 Publication

Catalytic activityi

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.1 Publication
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+.1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei183 – 1831Substrate; via carbonyl oxygenBy similarity
Binding sitei283 – 2831SubstrateBy similarity
Binding sitei319 – 3191FAD; shared with dimeric partnerBy similarity
Binding sitei330 – 3301FAD; shared with dimeric partnerBy similarity
Active sitei414 – 4141Proton acceptorBy similarity
Binding sitei415 – 4151Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 18310FADBy similarity
Nucleotide bindingi207 – 2093FADBy similarity
Nucleotide bindingi387 – 3915FAD; shared with dimeric partnerBy similarity
Nucleotide bindingi416 – 4183FADBy similarity

GO - Molecular functioni

GO - Biological processi

  • acyl-CoA metabolic process Source: MGI
  • fatty acid beta-oxidation Source: RGD
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: GO_Central
  • fatty acid metabolic process Source: RGD
  • lipid homeostasis Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11692.
SABIO-RKP70584.
UniPathwayiUPA00660.

Chemistry

SwissLipidsiSLP:000001390.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2013. Acadsb.

Subcellular locationi

  • Mitochondrion matrix 1 Publication

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 432399Short/branched chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei278 – 2781N6-succinyllysineBy similarity
Modified residuei284 – 2841N6-acetyllysine; alternateBy similarity
Modified residuei284 – 2841N6-succinyllysine; alternateBy similarity
Modified residuei426 – 4261N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP70584.
PRIDEiP70584.

PTM databases

iPTMnetiP70584.
PhosphoSiteiP70584.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

Homotetramer.Curated

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027999.

Structurei

3D structure databases

ProteinModelPortaliP70584.
SMRiP70584. Positions 52-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 2302Substrate bindingBy similarity
Regioni291 – 2944Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0139. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP70584.
KOiK09478.
OrthoDBiEOG74FF0S.
PhylomeDBiP70584.
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]

Sequencei

Sequence statusi: Complete.

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

P70584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSAFQLWR AGGLLRRNFL THSSSWKIPP RVLKSSQPEA LLSVTNNALC
60 70 80 90 100
FAPLQTFTDE DIMMQKAVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ
110 120 130 140 150
GMMGIEVEAK YGGTEASFLC SVLVIEELAK VDASVALLCD IQNTVINKLF
160 170 180 190 200
RKHGTEEQKA TYLPKLVTEK LGSFCLSEAG AGSDSFALKT RADKSGNYYV
210 220 230 240 250
INGSKMWISN AEHAELFLVF ANVDPPSGYR GITCFLVDRD TEGFQIGRRE
260 270 280 290 300
NKMGIRASST CQLTFENVKV PETSVLGKIG HGYKYAIGSL NEGRIGIAAQ
310 320 330 340 350
MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAHVA TQLEAARLLT
360 370 380 390 400
YNAARLVEAG RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV
410 420 430
EKFFRDAKIG TIYEGTSNIQ LNTIAKHIDA EY
Length:432
Mass (Da):47,824
Last modified:February 1, 1997 - v1
Checksum:iD35380C6DE3FC7DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64451 mRNA. Translation: AAB17136.1.
PIRiS71321.
RefSeqiNP_037216.1. NM_013084.2.
UniGeneiRn.44423.

Genome annotation databases

GeneIDi25618.
KEGGirno:25618.
UCSCiRGD:2013. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64451 mRNA. Translation: AAB17136.1.
PIRiS71321.
RefSeqiNP_037216.1. NM_013084.2.
UniGeneiRn.44423.

3D structure databases

ProteinModelPortaliP70584.
SMRiP70584. Positions 52-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027999.

Chemistry

SwissLipidsiSLP:000001390.

PTM databases

iPTMnetiP70584.
PhosphoSiteiP70584.

Proteomic databases

PaxDbiP70584.
PRIDEiP70584.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25618.
KEGGirno:25618.
UCSCiRGD:2013. rat.

Organism-specific databases

CTDi36.
RGDi2013. Acadsb.

Phylogenomic databases

eggNOGiKOG0139. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP70584.
KOiK09478.
OrthoDBiEOG74FF0S.
PhylomeDBiP70584.
TreeFamiTF105055.

Enzyme and pathway databases

UniPathwayiUPA00660.
BioCyciMetaCyc:MONOMER-11692.
SABIO-RKP70584.

Miscellaneous databases

PROiP70584.

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...

Publicationsi

  1. "Cloning of a cDNA for short/branched chain acyl-Coenzyme A dehydrogenase from rat and characterization of its tissue expression and substrate specificity."
    Willard J., Vicanek C., Battaile K.P., van Veldhoven P.P., Fauq A.H., Rozen R., Vockley J.
    Arch. Biochem. Biophys. 331:127-133(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-59.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Purification and characterization of 2-methyl-branched chain acyl coenzyme A dehydrogenase, an enzyme involved in the isoleucine and valine metabolism, from rat liver mitochondria."
    Ikeda Y., Tanaka K.
    J. Biol. Chem. 258:9477-9487(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACDSB_RAT
AccessioniPrimary (citable) accession number: P70584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.