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A8WP91 (ACAD2_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 40. 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 2, mitochondrial

Short name=MCAD
EC=1.3.8.7
Gene names
ORF Names:CBG00953
OrganismCaenorhabditis briggsae [Reference proteome]
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length408 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 – 55Mitochondrion Potential
Chain6 – 408403Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial UniProtKB Q22347
PRO_0000395328

Regions

Nucleotide binding143 – 15210FAD By similarity UniProtKB P11310
Nucleotide binding176 – 1783FAD By similarity UniProtKB P11310
Nucleotide binding291 – 2933FAD By similarity UniProtKB P11310
Nucleotide binding301 – 3022FAD By similarity UniProtKB P11310
Nucleotide binding355 – 3595FAD By similarity UniProtKB P11310
Nucleotide binding384 – 3863FAD By similarity UniProtKB P11310
Region263 – 2664Substrate binding By similarity UniProtKB P11310

Sites

Active site3821Proton acceptor By similarity UniProtKB P11310
Binding site1521Substrate; via carbonyl oxygen By similarity UniProtKB P11310
Binding site3831Substrate; via amide nitrogen By similarity UniProtKB P11310
Binding site3941Substrate By similarity UniProtKB P11310

Sequences

Sequence LengthMass (Da)Tools
A8WP91 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 0880122A2AB967D3

FASTA40844,608
        10         20         30         40         50         60 
MLSRLARTQI SRSALLSQTR QLSFDLNETQ KEIQAAALKF SKEVLVPNAA KFDESGEFPW 

        70         80         90        100        110        120 
EIIRQAHSLG LMNPQIPEKY GGPGMTTLET TLIVEALSYG CTGLQLGIMG PSLAIAPVYI 

       130        140        150        160        170        180 
AGNEEQKKKY LGALAAEPII ASYCVTEPGA GSDVNGVKTK CEKKGNEYII NGSKAWITGG 

       190        200        210        220        230        240 
GHAKWFFVLA RSDPNPKTPA GKAFTAFIVD GDTSGITRGK KEKNMGQRCS DTRTITFEDV 

       250        260        270        280        290        300 
RVPEENVLGP PGAGFKVAMS AFDMTRPGVA AGALGLSWRC LDESAKYALQ RKAFGTEIAN 

       310        320        330        340        350        360 
HQAVQFMLSD MAINLELARL ITYKSATDVD NGVRSSYNAS KSASQRIPRI RRLLMLFRCN 

       370        380        390        400 
GFNSEYPVEK LMRDAKIYQI YEGTSQIQRI VISRMLLGHV AQNGTSRM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE600951 Genomic DNA. Translation: CAP22297.2.

3D structure databases

ProteinModelPortalA8WP91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6238.CBG00953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCBG00953; CBG00953; CBG00953.

Organism-specific databases

WormBaseCBG00953; CBP35999; WBGene00024257.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131659.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACAD2_CAEBR
AccessionPrimary (citable) accession number: A8WP91
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: December 16, 2008
Last modified: November 13, 2013
This is version 40 of the entry and version 2 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