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Reviewed, UniProtKB/Swiss-Prot Q22347 (ACADM_CAEEL)

Last modified November 3, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3
Gene names
ORF Names: T08G2.3
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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.

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
   Technical termComplete proteome
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

acyl-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 – 1515Mitochondrion By similarity
Chain16 – 417402Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000507

Regions

Nucleotide binding148 – 15710FAD By similarity
Nucleotide binding181 – 1833FAD By similarity
Nucleotide binding306 – 3072FAD By similarity
Nucleotide binding364 – 3685FAD By similarity
Nucleotide binding393 – 3953FAD By similarity
Region268 – 2714Substrate binding By similarity

Sites

Active site3911Proton acceptor By similarity
Binding site1571Substrate; via carbonyl oxygen By similarity
Binding site3921Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q22347-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 98CE260E72C521BF

FASTA41744,818
        10         20         30         40         50         60 
MLSRIATSSL GLSRSATGVI ATQSRQISFD LSETQKEIQD AALKFSKDVL VPNAAKFDES 

        70         80         90        100        110        120 
GEFPWEIVRQ AHSLGLMNPQ IPEKYGGPGM TTLETALIVE ALSYGCTGIQ LGIMGPSLAI 

       130        140        150        160        170        180 
APVYISGNEE QKKKYLGALA AEPIIASYCV TEPGAGSDVN GVKTKCEKKG DEYIINGSKA 

       190        200        210        220        230        240 
WITGGGHAKW FFVLARSDPN PKTPAGKAFT AFIVDGDTPG ITRGKKEKNM GQRCSDTRVI 

       250        260        270        280        290        300 
TFEDVRVPAE NVLGAPGAGF KVAMEAFDMT RPGVAAGALG LSWRCLDESA KYALERKAFG 

       310        320        330        340        350        360 
TVIANHQAVQ FMLADMAVNL ELARLITYKS ANDVDNKVRS SYNASIAKCF AADTANQAAT 

       370        380        390        400        410 
NAVQIFGGNG FNSEYPVEKL MRDAKIYQIY EGTSQIQRIV ISRMLLGHFA QNGTSRI 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

U42838 Genomic DNA. Translation: AAB52493.1.
PIRT16838.
RefSeqNP_510788.1.
UniGeneCel.378

3D structure databases

HSSPHSSP built from PDB template 1EGE based on UniProtKB P11310.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:25385N.
IntActQ22347. 2 interactions.
STRINGQ22347.

Genome annotation databases

EnsemblT08G2.3.1; T08G2.3.1; T08G2.3; Caenorhabditis elegans. [Genome view]
T08G2.3.2; T08G2.3.2; T08G2.3; Caenorhabditis elegans. [Genome view]
GeneID181757.
KEGGcel:T08G2.3.
UCSCT08G2.3.1. c. elegans.

Organism-specific databases

CTD181757.
WormBaseWBGene00020366. T08G2.3.
WormPepT08G2.3. CE07473. [WorfDB]

Phylogenomic databases

OMASACCITE.

Enzyme and pathway databases

BRENDA1.3.99.3. 672.

Gene expression databases

ArrayExpressQ22347.

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...

Other Resources

NextBio915218.

Entry information

Entry nameACADM_CAEEL
AccessionPrimary (citable) accession number: Q22347
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 3, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

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