Reviewed, UniProtKB/Swiss-Prot Q9HZJ3 (FADA_PSEAE)

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:	PA3013

Organism

Pseudomonas aeruginosa [Complete proteome] [HAMAP]

Taxonomic identifier

287 [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
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_0000206378
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)
	Q9HZJ3-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: D04065FACB7E8A73	FASTA	391	41,643
	10 20 30 40 50 60 MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AETMSAHLIS KLLERNPKVD PAEVEDVIWG 70 80 90 100 110 120 CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIQ TGNGDVFVIG 130 140 150 160 170 180 GVEHMGHVGM MHGVDPNPHL SLYAAKASGM MGLTAEMLGK MHGISREAQD KFGARSHQLA 190 200 210 220 230 240 WKATQEGKFK DEIIPMEGYD ENGFLKVFDF DETIRPETTV ETLAELKPAF NPKGGTVTAG 250 260 270 280 290 300 TSSQITDGAS CMIVMSAQRA QDLGIQPMAV IRSMAVAGVD PAIMGYGPVP STNKALKRAG 310 320 330 340 350 360 LTIADIDFVE LNEAFAAQAL PVLKDLKLLD KMDEKVNLHG GAIALGHPFG CSGARISGTL 370 380 390 LNVMKQNGGT LGVSTMCVGL GQGITTVFER I

References

[1]

"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE004091 Genomic DNA. Translation: AAG06401.1.
PIR	F83269.
RefSeq	NP_251703.1.
3D structure databases
HSSP	HSSP built from PDB template 1PXT based on UniProtKB P27796.
SMR	Q9HZJ3. Positions 2-391.
ModBase	Search...
Genome annotation databases
GeneID	880523.
GenomeReviews	Gene locus PA3013 in contig AE004091_GR.
KEGG	pae:PA3013.
Organism-specific databases
PseudoCAP	PA3013.
CMR	Search...
Phylogenomic databases
HOGENOM	Q9HZJ3.
OMA	AIDDIYW.
Enzyme and pathway databases
BioCyc	PAER208964:PA3013-MON.
BRENDA	2.3.1.16. 354.
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_PSEAE

Accession

Primary (citable) accession number: Q9HZJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 52 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)