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Reviewed, UniProtKB/Swiss-Prot A4VKA4 (FADA_PSEU5)

Last modified November 3, 2009. Version 23. 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:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Fatty acid oxidation complex subunit beta
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
Gene names
Name: fadA
Synonyms: foaB
Ordered Locus Names: PST_1727
OrganismPseudomonas stutzeri (strain A1501) [Complete proteome] [HAMAP]
Taxonomic identifier379731 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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: HAMAP

lipid catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3913913-ketoacyl-CoA thiolase HAMAP MF_01620
PRO_0000323551

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A4VKA4-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 10443DF8691148DA

FASTA39141,738
        10         20         30         40         50         60 
MSLNPRDAVI VDFGRTPMGR SKGGMHRNTR AETMSAQLID GLLARNPKID PAEVEDVIWG 

        70         80         90        100        110        120 
CVNQTLEQGW NIARMASLLT RIPHTSAGQT VSRLCGSSMS ALHTAVQAIQ TNNGDVFVIG 

       130        140        150        160        170        180 
GVEHMGHVSM MHGVDPNPQL SLHAAKASGM MGLTAEMLGK MHGITREAQD QFGYRSHQLA 

       190        200        210        220        230        240 
WKATQEGKFK DEIIPMEGHD ENGFLKVFDY DETIRPETTL EGLAELKPAF NPKGGTVTAG 

       250        260        270        280        290        300 
TSSQITDGAS CMIVMSAQRA KDLGLQPMAV VRAMALAGVD PAIMGYGPVP STQKALKRAG 

       310        320        330        340        350        360 
LTMDDISHVE LNEAFAAQAL PVLKDLKLLD KMEEKVNLHG GAIALGHPFG CSGARISGTL 

       370        380        390 
LNVMKQNNGT LGVATMCIGL GQGISTVFER L 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y. expand/collapse author list , Elmerich C., Lin M., Jin Q.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000304 Genomic DNA. Translation: ABP79405.1.
RefSeqYP_001172247.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4VKA4.

Genome annotation databases

GeneID5097811.
GenomeReviewsGene locus PST_1727 in contig CP000304_GR.
KEGGpsa:PST_1727.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAKVFDYDE.

Family and domain databases

HAMAPMF_01620.
[Tree]
InterProIPR012805. FadA.
IPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. fadA. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADA_PSEU5
AccessionPrimary (citable) accession number: A4VKA4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 29, 2007
Last modified: November 3, 2009
This is version 23 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