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Reviewed, UniProtKB/Swiss-Prot P52042 (ACDS_CLOAB)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, short-chain specific
    EC=1.3.99.2
Alternative name(s):
    SCAD
    Butyryl-CoA dehydrogenase
Gene names
Name: bcd
Ordered Locus Names: CA_C2711
OrganismClostridium acetobutylicum [Complete proteome] [HAMAP]
Taxonomic identifier1488 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor.

Cofactor

FAD.

Pathway

Lipid metabolism; butyric acid metabolism.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

butyryl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: EC

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Acyl-CoA dehydrogenase, short-chain specific
PRO_0000201189

Sequences

Sequence LengthMass (Da)Tools
P52042-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4BC50A1991BD9FB2

FASTA37941,387
        10         20         30         40         50         60 
MDFNLTREQE LVRQMVREFA ENEVKPIAAE IDETERFPME NVKKMGQYGM MGIPFSKEYG 

        70         80         90        100        110        120 
GAGGDVLSYI IAVEELSKVC GTTGVILSAH TSLCASLINE HGTEEQKQKY LVPLAKGEKI 

       130        140        150        160        170        180 
GAYGLTEPNA GTDSGAQQTV AVLEGDHYVI NGSKIFITNG GVADTFVIFA MTDRTKGTKG 

       190        200        210        220        230        240 
ISAFIIEKGF KGFSIGKVEQ KLGIRASSTT ELVFEDMIVP VENMIGKEGK GFPIAMKTLD 

       250        260        270        280        290        300 
GGRIGIAAQA LGIAEGAFNE ARAYMKERKQ FGRSLDKFQG LAWMMADMDV AIESARYLVY 

       310        320        330        340        350        360 
KAAYLKQAGL PYTVDAARAK LHAANVAMDV TTKAVQLFGG YGYTKDYPVE RMMRDAKITE 

       370 
IYEGTSEVQK LVISGKIFR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824."
Boynton Z.L., Bennett G.N., Rudolph F.B.
J. Bacteriol. 178:3015-3024(1996) [PubMed: 8655474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[2]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

U17110 Genomic DNA. Translation: AAA95968.1.
AE001437 Genomic DNA. Translation: AAK80657.1.
PIRF97233.
T47262.
RefSeqNP_349317.1.

3D structure databases

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

Genome annotation databases

GeneID1118894.
GenomeReviewsGene locus CA_C2711 in contig AE001437_GR.
KEGGcac:CAC2711.
NMPDRfig|272562.1.peg.2846.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP52042.
OMAP52042. RGSATCE.

Enzyme and pathway databases

BioCycCACE272562:CAC2711-MON.
BRENDA1.3.99.2. 2866.

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 nameACDS_CLOAB
AccessionPrimary (citable) accession number: P52042
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 61 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

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