B1X9L5 (FADI_ECODH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase
EC=2.3.1.16

Alternative name(s):
ACSs
Acetyl-CoA acyltransferase
Acyl-CoA ligase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta

Gene names

Name:	fadI
Ordered Locus Names:	ECDH10B_2505

Organism

Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]

Taxonomic identifier

316385 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli › Escherichia coli (strain K12)

Protein attributes

Sequence length	436 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-Rule MF_01618
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP-Rule MF_01618
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01618
Subunit structure	Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI) 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 beta-oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 436	436	3-ketoacyl-CoA thiolase HAMAP-Rule MF_01618		PRO_1000185964
Sites
	Active site	99	1	Acyl-thioester intermediate By similarity
	Active site	392	1	Proton acceptor By similarity
	Active site	422	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1X9L5 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 5B89853172C16299	FASTA	436	46,531
	10 20 30 40 50 60 MGQVLPLVTR QGDRIAIVSG LRTPFARQAT AFHGIPAVDL GKMVVGELLA RSEIPAEVIE 70 80 90 100 110 120 QLVFGQVVQM PEAPNIAREI VLGTGMNVHT DAYSVSRACA TSFQAVANVA ESLMAGTIRA 130 140 150 160 170 180 GIAGGADSSS VLPIGVSKKL ARVLVDVNKA RTMSQRLKLF SRLRLRDLMP VPPAVAEYST 190 200 210 220 230 240 GLRMGDTAEQ MAKTYGITRE QQDALAHRSH QRAAQAWSDG KLKEEVMTAF IPPYKQPLVE 250 260 270 280 290 300 DNNIRGNSSL ADYAKLRPAF DRKHGTVTAA NSTPLTDGAA AVILMTESRA KELGLVPLGY 310 320 330 340 350 360 LRSYAFTAID VWQDMLLGPA WSTPLALERA GLTMSDLTLI DMHEAFAAQT LANIQLLGSE 370 380 390 400 410 420 RFAREALGRA HATGEVDDSK FNVLGGSIAY GHPFAATGAR MITQTLHELR RRGGGFGLVT 430 ACAAGGLGAA MVLEAE

References

[1]

"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000948 Genomic DNA. Translation: ACB03500.1.
RefSeq	YP_001731278.1. NC_010473.1.
3D structure databases
ProteinModelPortal	B1X9L5.
SMR	B1X9L5. Positions 17-435.
ModBase	Search...
Protein-protein interaction databases
STRING	316385.ECDH10B_2505.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB03500; ACB03500; ECDH10B_2505.
GeneID	6059897.
KEGG	ecd:ECDH10B_2505.
PATRIC	18464887. VBIEscCol59506_2530.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HOG000012240.
KO	K00632.
OMA	SKLESYA.
ProtClustDB	PRK08963.
Enzyme and pathway databases
BioCyc	ECOL316385:GJ8B-2407-MONOMER.
UniPathway	UPA00659.
Family and domain databases
Gene3D	3.40.47.10. 4 hits.
HAMAP	MF_01618. FadI.
InterPro	IPR012806. Ac-CoA_C-AcTrfase_FadI. 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]
PANTHER	PTHR18919. PTHR18919. 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. TIGR02446. FadI. 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

FADI_ECODH

Accession

Primary (citable) accession number: B1X9L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program