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Reviewed, UniProtKB/Swiss-Prot P45867 (ACDA_BACSU)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-CoA dehydrogenase
    EC=1.3.99.-
Gene names
Name: acdA
Synonyms: acd
Ordered Locus Names: BSU37170
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Acyl-CoA dehydrogenase
PRO_0000201182

Sequences

Sequence LengthMass (Da)Tools
P45867-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4D09861D59718EF9

FASTA37941,446
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

Z49782 Genomic DNA. Translation: CAA89868.1.
AL009126 Genomic DNA. Translation: CAB15745.1.
PIRS55421.
RefSeqNP_391598.1.

3D structure databases

HSSPHSSP built from PDB template 1BUC based on UniProtKB Q06319.
ModBaseSearch...

Genome annotation databases

GeneID938457.
GenomeReviewsGene locus BSU37170 in contig AL009126_GR.
KEGGbsu:BSU37170.
NMPDRfig|224308.1.peg.3724.

Organism-specific databases

SubtiListBG11239. acdA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP45867.
OMAP45867. EYARERH.

Enzyme and pathway databases

BioCycBSUB224308:BSU3715-MON.

Family and domain databases

InterProIPR006089. 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]
Gene3DG3DSA: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.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACDA_BACSU
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents