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P79273 (ACADS_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 99. 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
OrganismSus scrofa (Pig) [Reference proteome]
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 + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

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
   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 – 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 binding366 – 3705FAD; shared with dimeric partner By similarity
Nucleotide binding395 – 3973FAD By similarity
Region269 – 2724Substrate binding By similarity

Sites

Active site3931Proton 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 site3941Substrate; 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
P79273 [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 

« Hide

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

EMBL
GenBank
DDBJ
D89477 mRNA. Translation: BAA13964.1.
RefSeqNP_999063.1. NM_213898.1.
UniGeneSsc.14531.

3D structure databases

ProteinModelPortalP79273.
SMRP79273. Positions 34-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000010581.

Proteomic databases

PaxDbP79273.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396932.
KEGGssc:396932.

Organism-specific databases

CTD35.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131659.
HOVERGENHBG000224.
KOK00248.

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_PIG
AccessionPrimary (citable) accession number: P79273
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1997
Last modified: March 19, 2014
This is version 99 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