Reviewed, UniProtKB/Swiss-Prot Q54IM8 (ACAD8_DICDI)

Names and origin

Protein names

Recommended name:
    Isobutyryl-CoA dehydrogenase, mitochondrial
    EC=1.3.99.-
Alternative name(s):
    Acyl-CoA dehydrogenase family member 8 homolog

Gene names

Name:	acad8
ORF Names:	DDB_G0288647

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	416 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	Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism By similarity.
Catalytic activity	Isobutyryl-CoA + ETF = methylacrylyl-CoA + reduced ETF.
Cofactor	FAD By similarity.
Pathway	Amino-acid degradation; L-valine degradation.
Subunit structure	Homotetramer By similarity.
Subcellular location	MitochondrionBy similarity.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Activator Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro electron carrier activity 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 – 21	21	Mitochondrion Potential
	Chain	22 – 416	395	Isobutyryl-CoA dehydrogenase, mitochondrial		PRO_0000328143
Regions
	Nucleotide binding	155 – 165	11	FAD By similarity
	Nucleotide binding	370 – 376	7	FAD By similarity
	Nucleotide binding	399 – 401	3	FAD By similarity
	Region	273 – 276	4	Substrate binding By similarity
Sites
	Active site	397	1	Proton acceptor By similarity
	Binding site	301	1	FAD By similarity
	Binding site	409	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54IM8-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: BCA68ACB4C935C46	FASTA	416	45,694
	10 20 30 40 50 60 MISGLFKLSN KQSVLQNATK LVLQRRTFFN IVPNPSVGLT EDQKQFQSMA LDFAQEKMKP 70 80 90 100 110 120 FAEKWDKEEY FPRDVMREAA ELGFGGIYVR EDVGGSGLSR LDASIIIEAL ASADVSTTAF 130 140 150 160 170 180 ISIHNMCAGL IDIYGTEEQR KKFLPSLVSM EKIASYCLTE PGSGSDAGSL STKATKDGDH 190 200 210 220 230 240 YILNGSKAFI SGGGDSEVYL VMVRTGAEKG PKGISCLLVE KDTPGLSFGK KEEKLGWNTQ 250 260 270 280 290 300 PTRALIFEDC RVPVGNLIGK EGQGFSIAMN ALNGGRINIG ACSLGGAQSC LVAARDHVKV 310 320 330 340 350 360 RKQFNQPLEH FQAVQFKMAD MATKLHASRI MIRNAAAMLD AKDPSAHVYI AMAKLFACDE 370 380 390 400 410 CFKVTDDSLQ LFGGYGYLKD YPVERYLRDL RVHRILEGSD AVMRLIISRE LSKDDH

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000119 Genomic DNA. Translation: EAL63127.1.
RefSeq	XP_636630.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3388204.
KEGG	ddi:DDB_0237710.
Organism-specific databases
dictyBase	DDB_G0288647. acad8.
Family and domain databases
InterPro	IPR006091. Acyl-CoA_DHase/Oxase_M. IPR006089. Acyl-CoA_DHase_CS. IPR006092. Acyl-CoA_DHase_N. IPR006090. Acyl-CoA_Oxase/DHase_1. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA: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.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACAD8_DICDI

Accession

Primary (citable) accession number: Q54IM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)