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Protein

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadsb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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

FADBy similarity

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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-70895. Branched-chain amino acid catabolism.
UniPathwayiUPA00660.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1914135. Acadsb.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
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_0000000520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternateCombined sources
Modified residuei70 – 701N6-succinyllysine; alternateCombined sources
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei278 – 2781N6-succinyllysineCombined sources
Modified residuei284 – 2841N6-acetyllysine; alternateCombined sources
Modified residuei284 – 2841N6-succinyllysine; alternateCombined sources
Modified residuei426 – 4261N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBL1.
MaxQBiQ9DBL1.
PaxDbiQ9DBL1.
PRIDEiQ9DBL1.

PTM databases

iPTMnetiQ9DBL1.
PhosphoSiteiQ9DBL1.

Expressioni

Gene expression databases

BgeeiQ9DBL1.
ExpressionAtlasiQ9DBL1. baseline and differential.
GenevisibleiQ9DBL1. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9DBL1. 2 interactions.
MINTiMINT-1861281.
STRINGi10090.ENSMUSP00000015829.

Structurei

3D structure databases

ProteinModelPortaliQ9DBL1.
SMRiQ9DBL1. 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.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiQ9DBL1.
KOiK09478.
OrthoDBiEOG74FF0S.
PhylomeDBiQ9DBL1.
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.

Q9DBL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSALQLWR MGGLLRRRFP TCLSPWKIPP RVLKSSQPEA LVSLTNNAVA
60 70 80 90 100
FAPLQTLTDE EIMMKQTVKK FAQEHVAPLV SSMDENSKME KSVIQGLFQQ
110 120 130 140 150
GLMGIEVEAQ YGGTEASFFC SVLVIEELAK VDASVALLCD IQNTIINNLF
160 170 180 190 200
RKHASEEQKA TYLPKLVTEK LGSFCLSEAG AGSDSFAMKT RADKSGNYYV
210 220 230 240 250
LNGSKMWISH AEHAELFLVF ANVDPSSGYR GITCFLVDRD TEGFQIGKRE
260 270 280 290 300
NKMGIRASST CQLTFENVKV PETNILGKIG HGYKYAIGSL NEGRIGIAAQ
310 320 330 340 350
MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAQVA TQLEATRLLT
360 370 380 390 400
YNAARLVEAG RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV
410 420 430
EKFFRDAKIG TIYEGASNIQ LNTIAKHIDA EY
Length:432
Mass (Da):47,874
Last modified:June 1, 2001 - v1
Checksum:i0272723CE36BCC46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004889 mRNA. Translation: BAB23646.1.
CCDSiCCDS21916.1.
RefSeqiNP_080102.1. NM_025826.4.
UniGeneiMm.334274.
Mm.487956.

Genome annotation databases

EnsembliENSMUST00000015829; ENSMUSP00000015829; ENSMUSG00000030861.
GeneIDi66885.
KEGGimmu:66885.
UCSCiuc009kbm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004889 mRNA. Translation: BAB23646.1.
CCDSiCCDS21916.1.
RefSeqiNP_080102.1. NM_025826.4.
UniGeneiMm.334274.
Mm.487956.

3D structure databases

ProteinModelPortaliQ9DBL1.
SMRiQ9DBL1. Positions 52-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBL1. 2 interactions.
MINTiMINT-1861281.
STRINGi10090.ENSMUSP00000015829.

PTM databases

iPTMnetiQ9DBL1.
PhosphoSiteiQ9DBL1.

Proteomic databases

EPDiQ9DBL1.
MaxQBiQ9DBL1.
PaxDbiQ9DBL1.
PRIDEiQ9DBL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015829; ENSMUSP00000015829; ENSMUSG00000030861.
GeneIDi66885.
KEGGimmu:66885.
UCSCiuc009kbm.2. mouse.

Organism-specific databases

CTDi36.
MGIiMGI:1914135. Acadsb.

Phylogenomic databases

eggNOGiKOG0139. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiQ9DBL1.
KOiK09478.
OrthoDBiEOG74FF0S.
PhylomeDBiQ9DBL1.
TreeFamiTF105055.

Enzyme and pathway databases

UniPathwayiUPA00660.
ReactomeiR-MMU-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

NextBioi322929.
PROiQ9DBL1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBL1.
ExpressionAtlasiQ9DBL1. baseline and differential.
GenevisibleiQ9DBL1. MM.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 348-355, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-278 AND LYS-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-284 AND LYS-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACDSB_MOUSE
AccessioniPrimary (citable) accession number: Q9DBL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 124 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.