P21151 (FADA_ECOLI) 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
Synonyms:	oldA
Ordered Locus Names:	b3845, JW5578

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. Ref.9
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620
Pathway	Lipid metabolism; fatty acid beta-oxidation. Ref.9
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA).
Subcellular location	Cytoplasm HAMAP MF_01620.
Induction	Repressed by fadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to fadR resulting in its release from the DNA and thus derepression of the transcription. HAMAP MF_01620
Sequence similarities	Belongs to the thiolase family.
Biophysicochemical properties	Kinetic parameters: KM=96 µM for acetoacetyl-CoA Ref.8 KM=102 µM for CoASH

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference 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 – 387	387	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206372
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
Experimental info
	Sequence conflict	37	1	S → T in CAB40810. Ref.3
	Sequence conflict	37	1	S → T in AAA67642. Ref.4
	Sequence conflict	119	1	E → G in CAB40810. Ref.3
	Sequence conflict	371 – 374	4	TMCI → DGCVS AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P21151 [UniParc]. Last modified September 27, 2004. Version 3. Checksum: 1A60EF1E6C351704	FASTA	387	40,876
	10 20 30 40 50 60 MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH 130 140 150 160 170 180 MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT 190 200 210 220 230 240 QSAAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVN GMVTAGTSSA 250 260 270 280 290 300 LSDGAAAMLV MSESRAHELG LKPRARVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS 310 320 330 340 350 360 DIGVFEMNEA FAAQILPCIK DLGLIEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM 370 380 ERKDVQFGLA TMCIGLGQGI ATVFERV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes." Dirusso C.C. J. Bacteriol. 172:6459-6468(1990) [PubMed: 1699931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon." Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M. J. Biol. Chem. 265:10424-10429(1990) [PubMed: 2191949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: K12.
[3]	"Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nakahigashi K., Inokuchi H. Nucleic Acids Res. 18:4937-4937(1990) [PubMed: 2204034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed: 1379743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005." Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L. Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract] Cited for: SEQUENCE REVISION TO 37.
[7]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli." He X.Y., Yang S.Y. Biochemistry 35:9625-9630(1996) [PubMed: 8755745] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr. Mol. Microbiol. 47:793-805(2003) [PubMed: 12535077] [Abstract] Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M59368 Genomic DNA. Translation: AAA23751.1. M74164 Genomic DNA. Translation: AAA62778.1. X52837 Genomic DNA. Translation: CAB40810.1. M87049 Genomic DNA. Translation: AAA67642.1. U00096 Genomic DNA. Translation: AAT48230.1. AP009048 Genomic DNA. Translation: BAE77458.1.
PIR	XUEC. F65189.
RefSeq	YP_026272.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P21151.
SMR	P21151. Positions 1-387.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9559N.
2D gel databases
ECO2DBASE	H038.6. 6TH EDITION. H038.7. 6TH EDITION.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000043; EBESCP00000000043; EBESCG00000000035. EBESCT00000014885; EBESCP00000014176; EBESCG00000013945.
GeneID	948324.
GenomeReviews	Gene locus JW5578 in contig AP009048_GR. Gene locus b3845 in contig U00096_GR.
KEGG	ecj:JW5578. eco:b3845.
PATRIC	32123187. VBIEscCol129921_3959.
Organism-specific databases
EchoBASE	EB0274.
EcoGene	EG10278. fadA.
Phylogenomic databases
eggNOG	COG0183.
GeneTree	EBGT00050000009707.
HOGENOM	HBG370930.
OMA	AIDDIYW.
PhylomeDB	P21151.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	EcoCyc:FADA-MONOMER. MetaCyc:FADA-MONOMER.
Gene expression databases
Genevestigator	P21151.
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_ECOLI

Accession

Primary (citable) accession number: P21151
Secondary accession number(s): P78130, Q2M8E8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	September 27, 2004
Last modified:	January 25, 2012
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program