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A8XNF0 (ACAD1_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 42. 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:
Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial

Short name=MCAD
EC=1.3.8.7
Gene names
ORF Names:CBG15946
OrganismCaenorhabditis briggsae [Reference proteome]
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme is specific for acyl chain lengths of 4 to 16 By similarity. UniProtKB P11310

Catalytic activity

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactor

FAD By similarity. UniProtKB P11310

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation. UniProtKB P11310

Subunit structure

Homotetramer By similarity. UniProtKB P11310

Subcellular location

Mitochondrion matrix By similarity UniProtKB P11310.

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
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

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 – 1313Mitochondrion Potential
Chain14 – 417404Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial UniProtKB Q22347
PRO_0000395327

Regions

Nucleotide binding148 – 15710FAD By similarity UniProtKB P11310
Nucleotide binding181 – 1833FAD By similarity UniProtKB P11310
Nucleotide binding296 – 2983FAD By similarity UniProtKB P11310
Nucleotide binding306 – 3072FAD By similarity UniProtKB P11310
Nucleotide binding364 – 3685FAD By similarity UniProtKB P11310
Nucleotide binding393 – 3953FAD By similarity UniProtKB P11310
Region268 – 2714Substrate binding By similarity UniProtKB P11310

Sites

Active site3911Proton acceptor By similarity UniProtKB P11310
Binding site1571Substrate; via carbonyl oxygen By similarity UniProtKB P11310
Binding site3921Substrate; via amide nitrogen By similarity UniProtKB P11310
Binding site4031Substrate By similarity UniProtKB P11310

Sequences

Sequence LengthMass (Da)Tools
A8XNF0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: A21A018375E2C863

FASTA41744,669
        10         20         30         40         50         60 
MLSRFATTSL GLSRSATGVL ASQSRQISFD LSDTQKEIQA AALKFSKEVL VPNAAKFDES 

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

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

       190        200        210        220        230        240 
WITGGGHAKW FFVLARSDSD PKAPAGKAFT AFIVDGDTPG ISRGKKEKNM GQRCSDTRTI 

       250        260        270        280        290        300 
TFEDVRVPAE NVLGAPGAGF KVAMGAFDMT RPGVAAGALG LAWRCLDESA KYALQRKAFG 

       310        320        330        340        350        360 
TEIANHQAVQ FMLADMAVNL ELARLITYKS ATDVDNKVRS SYNASIAKCF AADTANQAAT 

       370        380        390        400        410 
NAVQIFGGNG FNSEYPVEKL MRDAKIYQIY EGTSQIQRIV ISRMLLGHFA QNGTSRI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE600995 Genomic DNA. Translation: CAP34381.1.
RefSeqXP_002643349.1. XM_002643303.1.

3D structure databases

ProteinModelPortalA8XNF0.
SMRA8XNF0. Positions 28-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6238.CBG15946.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCBG15946; CBG15946; CBG15946.
GeneID8585343.
KEGGcbr:CBG15946.

Organism-specific databases

CTD8585343.
WormBaseCBG15946; CBP23278; WBGene00036045.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131659.
KOK00249.
OMAIAMGTFD.
OrthoDBEOG74FF0S.

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 nameACAD1_CAEBR
AccessionPrimary (citable) accession number: A8XNF0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: January 15, 2008
Last modified: November 13, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways