Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q87ZB3 (FADA_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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:PSPTO_3516
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [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_0000206386

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q87ZB3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E0572722AF7EBE9B

FASTA39141,720
        10         20         30         40         50         60 
MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNNKVD PAEVEDVIWG 

        70         80         90        100        110        120 
CVNQTLEQGW NIARMASLLT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TNNGDVFVIG 

       130        140        150        160        170        180 
GVEHMGHVSM MHGVDPNPHM SLHAAKASGM MGLTAEMLGK MHGITREQQD AFGLRSHQLA 

       190        200        210        220        230        240 
HKATLEGKFK DEIIPMQGYD ENGFLRVFDY DETIRPDTTL ESLAALKPAF NPKGGTVTAG 

       250        260        270        280        290        300 
TSSQITDGAS CMIVMSAQRA QDLGIQPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG 

       310        320        330        340        350        360 
LSISDIDFFE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG CSGARISGTL 

       370        380        390 
LNVMKQNGGT FGVSTMCIGL GQGIATVFER V 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO56991.1.
RefSeqNP_793296.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ87ZB3.
SMRQ87ZB3. Positions 2-391.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1185181.
GenomeReviewsGene locus PSPTO_3516 in contig AE016853_GR.
KEGGpst:PSPTO_3516.
NMPDRfig|223283.1.peg.3434.
PATRIC19998459. VBIPseSyr93040_3601.
TIGRPSPTO_3516.

Phylogenomic databases

HOGENOMHBG370930.
OMATNNGDVF.
ProtClustDBPRK08947.

Enzyme and pathway databases

BioCycPSYR223283:PSPTO_3516-MONOMER.

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.
IPR020610. Thiolase_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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADA_PSESM
AccessionPrimary (citable) accession number: Q87ZB3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 60 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