Reviewed, UniProtKB/Swiss-Prot P45867 (ACDA_BACSU)

Names and origin

Protein names

Recommended name:
    Acyl-CoA dehydrogenase
    EC=1.3.99.-

Gene names

Name:	acdA
Synonyms:	acd
Ordered Locus Names:	BSU37170

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in the degradation of long-chain fatty acids.
Catalytic activity	Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF.
Cofactor	FAD By similarity.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Induction	Repressed by fadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize fadR as to its binding to fadR boxes on target DNA and thus derepress transcription. Ref.3
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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
	Chain	1 – 379	379	Acyl-CoA dehydrogenase		PRO_0000201182

Sequences

	Sequence		Length	Mass (Da)
	P45867-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4D09861D59718EF9	FASTA	379	41,446
	10 20 30 40 50 60 MNFSLSEEHE MIRKLVRDFA KHEVAPTAAE RDEQERFDRE LFREMANLGL TGIPWPEDYG 70 80 90 100 110 120 GIGSDYLAYV IAVEELSKVC ASTGVTLSAH ISLCSWPLFA FGTEEQKTEY LTQLALGEKI 130 140 150 160 170 180 GAFALTEAGS GSDAGSMKTT AERIGDDYVL NGSKVFITNG GVADIYIVFA VTDPEKKKKG 190 200 210 220 230 240 VTAFIVEKDF EGFFTGKKEK KLGIRSSPTT EIMFEDCVVP ASKRLGEEGE GFKIAMKTLD 250 260 270 280 290 300 GGRNGIAAQA VGIAQGALDA ALQYAKERKQ FGKSIAEQQG IAFKLADMAT MIEASRLLTY 310 320 330 340 350 360 QAAWLESSGL PYGKASAMSK LMAGDTAMKV TTEAVQIFGG YGYTKDYPVE RYMRDAKITQ 370 IYEGTQEIQR LVISRMLAD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation." Matsuoka H., Hirooka K., Fujita Y. J. Biol. Chem. 282:5180-5194(2007) [PubMed: 17189250] [Abstract] Cited for: GENE NAME, INDUCTION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49782 Genomic DNA. Translation: CAA89868.1. AL009126 Genomic DNA. Translation: CAB15745.1.
PIR	S55421.
RefSeq	NP_391598.1.
3D structure databases
HSSP	HSSP built from PDB template 1BUC based on UniProtKB Q06319.
ModBase	Search...
Genome annotation databases
GeneID	938457.
GenomeReviews	Gene locus BSU37170 in contig AL009126_GR.
KEGG	bsu:BSU37170.
NMPDR	fig|224308.1.peg.3724.
Organism-specific databases
SubtiList	BG11239. acdA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P45867.
OMA	P45867. EYARERH.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3715-MON.
Family and domain databases
InterPro	IPR006089. 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]
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

ACDA_BACSU

Accession

Primary (citable) accession number: P45867

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)