Reviewed, UniProtKB/Swiss-Prot A7ZU50 (FADA_ECO24)

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:	EcE24377A_4364

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	387 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 – 387	387	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000323545
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity
	Active site	343	1	Proton acceptor By similarity
	Active site	373	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZU50-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: FB4476C1218989D8	FASTA	387	40,833
	10 20 30 40 50 60 MEQVVIVDAI RTPMSRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMSGDA QACLVGGVEH 130 140 150 160 170 180 MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT 190 200 210 220 230 240 QSGAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVS GTVTAGTSSA 250 260 270 280 290 300 LSDGAAAMLV MSESRAHELG LKPRARVRSM AVVGCDPAIM GYGPVPASKL ALKKAGLSVS 310 320 330 340 350 360 DIGVFEMNEA FAAQILPCIK DLGLIEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM 370 380 ERKDVQFGLA TMCIGLGQGI ATVFERV

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000800 Genomic DNA. Translation: ABV20513.1.
RefSeq	YP_001465329.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZU50.
Genome annotation databases
GeneID	5587876.
GenomeReviews	Gene locus EcE24377A_4364 in contig CP000800_GR.
KEGG	ecw:EcE24377A_4364.
NMPDR	fig|331111.3.peg.1991.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	AIDDIYW.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADA_ECO24

Accession

Primary (citable) accession number: A7ZU50

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 19 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)