Q3K9D9 (FADA_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	Pfl01_3878

Organism

Pseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]

Taxonomic identifier

205922 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
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. 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 process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC
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_0000292897
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)
	Q3K9D9 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 14B93EC8C6DC9D4F	FASTA	391	41,623
	10 20 30 40 50 60 MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNTKVD PAEVEDVIWG 70 80 90 100 110 120 CVNQTLEQGW NIARMASLMT QIPHTSAGQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVVG 130 140 150 160 170 180 GVEHMGHVSM MHGVDPNPHM SLYAAKASGM MGLTAEMLGK MHGITREQQD AFGVRSHQLA 190 200 210 220 230 240 HKATVEGKFK DEIIPMQGYD ENGFLKTFDY DETIRPETTL ESLAALKPAF NPKGGTVTAG 250 260 270 280 290 300 TSSQITDGAS CMIVMSAQRA QDLGIQPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG 310 320 330 340 350 360 LGINDIDFFE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG CSGARISGTL 370 380 390 LNVMKQNGGT FGVATMCIGL GQGISTVFER V

References

[1]

"Genomic and genetic analyses of diversity and plant interactions of Pseudomonas fluorescens." Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., Harris S., Challis G.L., Yaxley A.M., Harris D. , Seeger K., Murphy L., Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., Parkhill J., Levy S.B., Rainey P.B., Thomson N.R. Genome Biol. 10:R51.1-R51.16(2009) [PubMed: 19432983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pf0-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000094 Genomic DNA. Translation: ABA75615.1.
RefSeq	YP_349606.1. NC_007492.2.
3D structure databases
HSSP	HSSP built from PDB template 2D3T based on UniProtKB P28790.
ProteinModelPortal	Q3K9D9.
SMR	Q3K9D9. Positions 2-391.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3K9D9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3712524.
GenomeReviews	Gene locus Pfl01_3878 in contig CP000094_GR.
KEGG	pfo:Pfl01_3878.
PATRIC	19889857. VBIPseFlu44242_3873.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	SSMEAIH.
PhylomeDB	Q3K9D9.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	PFLU205922:PFL_3878-MONOMER.
Family and domain databases
HAMAP	MF_01620. FadA. [Tree]
InterPro	IPR012805. 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]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KO	K00632.
PANTHER	PTHR18919:SF35. PTHR18919:SF35. 1 hit. 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.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADA_PSEPF

Accession

Primary (citable) accession number: Q3K9D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program