Reviewed, UniProtKB/Swiss-Prot Q6FF69 (FADA_ACIAD)

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:	ACIAD0334

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	390 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 – 390	390	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206368
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	346	1	Proton acceptor By similarity
	Active site	376	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FF69-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: D8E3050256548E62	FASTA	390	41,215
	10 20 30 40 50 60 MTNLNPRDVV IVDGVRSAMG KSKNGMFRNV RADSLSAELV RALVARNQFD VNEVEDLIWG 70 80 90 100 110 120 CVNQTLEQGM NIGRNIVLLA DLPKTVAGQT VNRLCGSSMQ AIHTAAAQIA TNQGDIFIIG 130 140 150 160 170 180 GVEHMGHVGM MHGIDLNPEA SKHYAKASNM MGLTAEMLGR MNGIGREEQD AFGVESHRRA 190 200 210 220 230 240 WAATQEGRFK NEIVGVEGHD ANGFKILCDI DEVIRPDANL EAFKALRPVF DPKGGTVTAA 250 260 270 280 290 300 TSSALSDGAS AMLLMSAERA QALGLKPRAV IRSMAVAGCD AAIMGYGPVP ATQKALKRAG 310 320 330 340 350 360 LSVADIQTVE LNEAFAAQGL SVLKGLGLYE KQDIVNLNGG AIALGHPLGC SGARITTTLL 370 380 390 NVMEQQDTQI GLATMCIGLG QGIATVIERV

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG67288.1.
RefSeq	YP_045110.1.
3D structure databases
SMR	Q6FF69. Positions 3-390.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FF69.
Genome annotation databases
GeneID	2881153.
GenomeReviews	Gene locus ACIAD0334 in contig CR543861_GR.
KEGG	aci:ACIAD0334.
NMPDR	fig|62977.3.peg.811.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	KVFDYDE.
PhylomeDB	Q6FF69.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0334-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. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADA_ACIAD

Accession

Primary (citable) accession number: Q6FF69

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 42 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)