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Reviewed, UniProtKB/Swiss-Prot P79273 (ACADS_PIG)

Last modified September 1, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Short-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=SCAD
    EC=1.3.99.2
Alternative name(s):
    Butyryl-CoA dehydrogenase
Gene names
Name: ACADS
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length413 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 + acceptor = 2-butenoyl-CoA + reduced acceptor.

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

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
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

butyryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: EC

electron carrier activity

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 – 413389Short-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000500

Regions

Nucleotide binding152 – 16110FAD By similarity
Nucleotide binding185 – 1873FAD By similarity
Nucleotide binding366 – 3705FAD By similarity
Nucleotide binding395 – 3973FAD By similarity

Sites

Active site3931Proton acceptor By similarity
Binding site2971FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P79273-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: B8C480ADEFDF7E98

FASTA41344,851
        10         20         30         40         50         60 
MAAALLARAC GPVRGALWPR DCRRLHTIFQ SVELPETYQM LRQTCRDFAE KELVPIAAQV 

        70         80         90        100        110        120 
DKEHRFPEAQ VKKMGELGLM AMDVPEELSG AGLDYLAYTI AMEEISRGCA STGVIMSVNN 

       130        140        150        160        170        180 
FLYLGPILKF GSKEQKQQWI TPFTSGDKVG CFALSEPGNG SDAGAAATTA QADHDSWVLS 

       190        200        210        220        230        240 
GTKAWITNAW EASAAVVFAS TDRSLQNKGI SAFLVPMPTA GLTLGKKEDK LGIRASSTAN 

       250        260        270        280        290        300 
LIFEDCRIPK ENLLGEPGMG FKIAMKTLDM GRIGIASKAL GISQAALDCA VNYAENRRAF 

       310        320        330        340        350        360 
GVPLTKLQGI QFKLADMALA LESARLLTWR AAMLKDNKKN PFIKEPAMAK LAASEAATAI 

       370        380        390        400        410 
THQAIQILGG MGYVTEMPAE RHYRDARITE IYEGTSEIQR LVIAGHLLKS YRS 

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References

[1]"Isolation of the pig short-chain acyl-CoA dehydrogenase gene and assignment to chromosome 14q16.2-q23.2."
Suzuki H., Itoh T., Kimura M., Murakami Y., Hamasima N., Yasue H.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

D89477 mRNA. Translation: BAA13964.1.
RefSeqNP_999063.1.
UniGeneSsc.14531

3D structure databases

HSSPHSSP built from PDB template 1JQI based on UniProtKB P15651.
SMRP79273. Positions 28-412.
ModBaseSearch...

Genome annotation databases

GeneID396932.
KEGGssc:396932.

Organism-specific databases

CTD396932.

Phylogenomic databases

HOVERGENP79273.

Enzyme and pathway databases

BRENDA1.3.99.2. 249.

Family and domain databases

InterProIPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_M.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACADS_PIG
AccessionPrimary (citable) accession number: P79273
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1997
Last modified: September 1, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents