Reviewed, UniProtKB/Swiss-Prot Q1I7D5 (FADA_PSEE4)

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
Ordered Locus Names:	PSEEN3727

Organism

Pseudomonas entomophila (strain L48) [Complete proteome] [HAMAP]

Taxonomic identifier

384676 [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. HAMAP MF_01620
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: 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_0000292896
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)
	Q1I7D5-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: E13D46C96DEA05F1	FASTA	391	41,646
	10 20 30 40 50 60 MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNDKID PKEVEDVIWG 70 80 90 100 110 120 CVNQTMEQGW 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]

"Complete genome sequence of the entomopathogenic and metabolically versatile soil bacterium Pseudomonas entomophila." Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F. Nat. Biotechnol. 24:673-679(2006) [PubMed: 16699499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT573326 Genomic DNA. Translation: CAK16447.1.
RefSeq	YP_609234.1.
3D structure databases
SMR	Q1I7D5. Positions 2-391.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1I7D5.
Genome annotation databases
GeneID	4090408.
GenomeReviews	Gene locus PSEEN3727 in contig CT573326_GR.
KEGG	pen:PSEEN3727.
NMPDR	fig|384676.6.peg.3200.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	SSMEAIH.
PhylomeDB	Q1I7D5.
Enzyme and pathway databases
BioCyc	PENT384676:PSEEN3727-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. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [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_PSEE4

Accession

Primary (citable) accession number: Q1I7D5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 13, 2006
Last modified:	February 9, 2010
This is version 32 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)