Reviewed, UniProtKB/Swiss-Prot Q9R9W0 (FADA_PSEPU)

Names and origin

Protein names

Recommended 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

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: HAMAP lipid catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206382
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	347	1	Proton acceptor By similarity
	Active site	377	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9R9W0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: EEB2DCE65EAE51D6	FASTA	391	41,614
	10 20 30 40 50 60 MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNDKVD PKEVEDVIWG 70 80 90 100 110 120 CVNQTLEQGW NIARMASLMT PIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVIG 130 140 150 160 170 180 GVEHMGHVSM MHGVDPNPHL SLHAAKASGM MGLTAEMLGK MHGITREQQD LFGVRSHQLA 190 200 210 220 230 240 HKATVEGKFK DEIIPMQGYD ENGFLKVFDF DETIRPETTL EGLASLKPAF NPKGGTVTAG 250 260 270 280 290 300 TSSQITDGAS CMIVMSGQRA MDLGIQPLAV IRSMAVAGVD PAIMGYGPVP STQKALKRAG 310 320 330 340 350 360 LTMADIDFIE LNEAFAAQAL PVLKDLKVLD KMDEKVNLHG GAIALGHPFG CSGARISGTL 370 380 390 LNVMKQNGGT LGVATMCVGL GQGITTVFER V

References

[1]

"Novel biodegradable aromatic plastics from a bacterial source. Genetic and biochemical studies on a route of the phenylacetyl-CoA catabolon." Garcia B., Olivera E.R., Minambres B., Fernandez-Valverde M., Canedo L.M., Prieto M.A., Garcia J.L., Martinez M., Luengo J.M. J. Biol. Chem. 274:29228-29241(1999) [PubMed: 10506180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: U.

[2]

"Two different pathways are involved in the beta-oxidation of n-alkanoic and n-phenylalkanoic acids in Pseudomonas putida U: genetic studies and biotechnological applications." Olivera E.R., Carnicero D., Garcia B., Minambres B., Moreno M.A., Canedo L., Dirusso C.C., Naharro G., Luengo J.M. Mol. Microbiol. 39:863-874(2001) [PubMed: 11251808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: U.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF150672 Genomic DNA. Translation: AAF02534.1. AF290949 Genomic DNA. Translation: AAK18168.1.
3D structure databases
HSSP	HSSP built from PDB template 1DLU based on UniProtKB P07097.
SMR	Q9R9W0. Positions 2-391.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.16. 403.
Family and domain databases
HAMAP	MF_01620. [Tree]
InterPro	IPR012805. FadA. IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit. TIGR02445. fadA. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADA_PSEPU

Accession

Primary (citable) accession number: Q9R9W0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)