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Reviewed, UniProtKB/Swiss-Prot Q3SZB4 (ACADM_BOVIN)

Last modified January 19, 2010. Version 42. 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

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Names and origin

Protein namesRecommended name:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3
Gene names
Name: ACADM
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

This enzyme is specific for acyl chain lengths of 4 to 16 By similarity.

Catalytic activity

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

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.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

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

acyl-CoA dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion By similarity
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000281995

Regions

Nucleotide binding158 – 16710FAD By similarity
Nucleotide binding191 – 1933FAD By similarity
Nucleotide binding306 – 3083FAD By similarity
Nucleotide binding316 – 3172FAD By similarity
Nucleotide binding374 – 3785FAD By similarity
Nucleotide binding403 – 4053FAD By similarity
Region278 – 2814Substrate binding By similarity

Sites

Active site4011Proton acceptor By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Binding site4021Substrate; via amide nitrogen By similarity
Binding site4131Substrate By similarity

Amino acid modifications

Modified residue2121N6-acetyllysine By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue3011N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q3SZB4-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: C43979D54E7A3A8D

FASTA42146,573
        10         20         30         40         50         60 
MIALFRRSCG VLRSLSHFDW RSQHTKTALQ REPGSGFSFE FTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPLAAEYDKT GEYPVPLIKR AWELGLMNTH IPESCGGLGL GTFDSCLISE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANSLGQ MPVIIAGNDQ QQKKYLGRMT EEPLMCAYCV TEPVAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVRVPKE NVLIGEGAGF KIAMGAFDKT RPPVAAAAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALERKTFG KLLIEHQGIS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAY 

       370        380        390        400        410        420 
AGDIANQLAS DAVQIFGGNG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIGRYK 


K

« Hide

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References

« Hide 'large scale' references
[1]"Association of bovine ACADM SNP with economic traits."
Li H., Xu S., Gao X., Ren H., Li J.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Heart ventricle.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EU009460 mRNA. Translation: ABS70460.1.
BC102989 mRNA. Translation: AAI02990.1.
IPIIPI00704474.
RefSeqNP_001068703.1.
UniGeneBt.61205

3D structure databases

HSSPHSSP built from PDB template 1WS9 based on UniProtKB Q5SGZ2.
SMRQ3SZB4. Positions 36-420.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SZB4.

Genome annotation databases

EnsemblENSBTAT00000033470; ENSBTAP00000033383; ENSBTAG00000024240; Bos taurus. [Genome view]
GeneID505968.
KEGGbta:505968.

Organism-specific databases

CTD505968.

Phylogenomic databases

eggNOGmaNOG08345.
HOVERGENQ3SZB4.
InParanoidQ3SZB4.
OMADQQKKKY.
OrthoDBEOG9FFGM4.

Enzyme and pathway databases

BRENDA1.3.99.3. 251.

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_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
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...

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Entry information

Entry nameACADM_BOVIN
AccessionPrimary (citable) accession number: Q3SZB4
Secondary accession number(s): A7LFV4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: January 19, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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