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A6V383 (FADA_PSEA7) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase

EC=2.3.1.16
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta
Gene names
Name:fadA
Ordered Locus Names:PSPA7_2146
OrganismPseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]
Taxonomic identifier381754 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP MF_01620

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620

Subunit structure

Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_01620.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3913913-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000323548

Sites

Active site951Acyl-thioester intermediate By similarity
Active site3471Proton acceptor By similarity
Active site3771Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A6V383 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 0CF3E0FEDB2FC33B

FASTA39141,628
        10         20         30         40         50         60 
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AETMSAHLIS KLLERNPKVD PAEVEDVIWG 

        70         80         90        100        110        120 
CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIQ TGNGDVFVIG 

       130        140        150        160        170        180 
GVEHMGHVGM MHGVDPNPHL SLYAAKASGM MGLTAEMLGK MHGISREAQD KFGARSHQLA 

       190        200        210        220        230        240 
WKATQEGKFK DEIIPMEGYD ENGFLKVFDF DETIRPETTV ETLAQLKPAF NPKGGTVTAG 

       250        260        270        280        290        300 
TSSQITDGAS CMIVMSAQRA QDLGIQPMAV IRSMAVAGVD PAIMGYGPVP STNKALKRAG 

       310        320        330        340        350        360 
LTIADIDFVE LNEAFAAQAL PVLKDLKLLD KMDEKVNLHG GAIALGHPFG CSGARISGTL 

       370        380        390 
LNVMKQNGGT LGVSTMCVGL GQGITTVFER V 

« Hide

References

[1]Dodson R.J., Harkins D., Paulsen I.T.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PA7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000744 Genomic DNA. Translation: ABR80694.1.
RefSeqYP_001347518.1. NC_009656.1.

3D structure databases

ProteinModelPortalA6V383.
SMRA6V383. Positions 2-391.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6V383.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5359206.
GenomeReviewsGene locus PSPA7_2146 in contig CP000744_GR.
KEGGpap:PSPA7_2146.
PATRIC19826074. VBIPseAer80442_2061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHBG370930.
OMAAIDDIYW.
PhylomeDBA6V383.
ProtClustDBPRK08947.

Family and domain databases

HAMAPMF_01620. FadA.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KOK00632.
PANTHERPTHR18919:SF35. PTHR18919:SF35. 1 hit.
PTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. FadA. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADA_PSEA7
AccessionPrimary (citable) accession number: A6V383
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: August 21, 2007
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families