A8WP91 (ACAD2_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial
Short name=MCAD
EC=1.3.8.7

Gene names

ORF Names:

CBG00953

Organism

Caenorhabditis briggsae [Reference proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acyl-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 5	5	Mitochondrion Potential
	Chain	6 – 408	403	Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial UniProtKB Q22347		PRO_0000395328
Regions
	Nucleotide binding	143 – 152	10	FAD By similarity UniProtKB P11310
	Nucleotide binding	176 – 178	3	FAD By similarity UniProtKB P11310
	Nucleotide binding	291 – 293	3	FAD By similarity UniProtKB P11310
	Nucleotide binding	301 – 302	2	FAD By similarity UniProtKB P11310
	Nucleotide binding	355 – 359	5	FAD By similarity UniProtKB P11310
	Nucleotide binding	384 – 386	3	FAD By similarity UniProtKB P11310
	Region	263 – 266	4	Substrate binding By similarity UniProtKB P11310
Sites
	Active site	382	1	Proton acceptor By similarity UniProtKB P11310
	Binding site	152	1	Substrate; via carbonyl oxygen By similarity UniProtKB P11310
	Binding site	383	1	Substrate; via amide nitrogen By similarity UniProtKB P11310
	Binding site	394	1	Substrate By similarity UniProtKB P11310

Sequences

	Sequence		Length	Mass (Da)
	A8WP91 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 0880122A2AB967D3	FASTA	408	44,608
	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

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	HE600951 Genomic DNA. Translation: CAP22297.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	6238.CBG00953.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	CBG00953; CBG00953; CBG00953.
Organism-specific databases
WormBase	CBG00953; CBP35999; WBGene00024257.
Phylogenomic databases
eggNOG	COG1960.
HOGENOM	HOG000131659.
Enzyme and pathway databases
UniPathway	UPA00660.
Family and domain databases
Gene3D	1.10.540.10. 1 hit. 2.40.110.10. 1 hit.
InterPro	IPR006089. 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. [Graphical view]
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit.
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACAD2_CAEBR

Accession

Primary (citable) accession number: A8WP91

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	December 16, 2008
Last modified:	April 3, 2013
This is version 37 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project