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Q5RAS0 (ACADS_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Short name=SCAD
EC=1.3.8.1
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene names
Name:ACADS
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

butyryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion By similarity
Chain25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000290193

Regions

Nucleotide binding152 – 16110FAD By similarity
Nucleotide binding185 – 1873FAD By similarity
Nucleotide binding365 – 3695FAD By similarity
Nucleotide binding365 – 3695FAD; shared with dimeric partner By similarity
Nucleotide binding394 – 3963FAD By similarity
Region269 – 2724Substrate binding By similarity

Sites

Active site3921Proton acceptor By similarity
Binding site1611Substrate; via carbonyl oxygen By similarity
Binding site2971FAD By similarity
Binding site2971FAD; shared with dimeric partner By similarity
Binding site3081FAD By similarity
Binding site3931Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue511N6-acetyllysine; alternate By similarity
Modified residue511N6-succinyllysine; alternate By similarity
Modified residue721N6-acetyllysine By similarity
Modified residue1291N6-acetyllysine; alternate By similarity
Modified residue1291N6-succinyllysine; alternate By similarity
Modified residue2081N6-acetyllysine By similarity
Modified residue2621N6-acetyllysine; alternate By similarity
Modified residue2621N6-succinyllysine; alternate By similarity
Modified residue3061N6-acetyllysine; alternate By similarity
Modified residue3061N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RAS0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 7192364FDD45CF4C

FASTA41244,435
        10         20         30         40         50         60 
MAAALLARAS GPVRRALRPR AWRQLHTIYQ SVELPETHQM LLQTCRDFAE KELFPIAAQV 

        70         80         90        100        110        120 
DKEHLFPAAQ VKKMGGLGLL AMDVPEELGG AGLDYLAYAI AMEEISRGCA STGVIMSVNN 

       130        140        150        160        170        180 
SLYLGPILKF GSKEQKQKWV TPFTSGDKIG CFALSEPGNG SDAGAASTTA RAEGDSWVLN 

       190        200        210        220        230        240 
GTKAWITNAW EASAAVVFAS TDRALQNKGI SAFLVPMPTP GLTLGKKEDK LGIRGSSTAN 

       250        260        270        280        290        300 
LIFEDCRIPK DSILGEPGMG FKIAMQTLDM GRIGIASQAL GIAQTALDCA VNYAENRMAF 

       310        320        330        340        350        360 
GAPLTKLQVI QFKLADMALA LESARLLTWR AAMLKDNKKP FIKEAAMAKL AASEAATAIS 

       370        380        390        400        410 
HQAIQILGGM GYVTEMPAER HYRDARITEI YEGTSEIQRL VIAGHLLRSY RS 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858942 mRNA. Translation: CAH91140.1.
UniGenePab.9153.

3D structure databases

ProteinModelPortalQ5RAS0.
SMRQ5RAS0. Positions 34-412.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RAS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000224.

Enzyme and pathway databases

UniPathwayUPA00660.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. 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]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACADS_PONAB
AccessionPrimary (citable) accession number: Q5RAS0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways