B2VFE0 (FADA_ERWT9) 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
Ordered Locus Names:	ETA_02450

Organism

Erwinia tasmaniensis (strain DSM 17950 / Et1/99) [Complete proteome] [HAMAP]

Taxonomic identifier

338565 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Erwinia

Protein attributes

Sequence length	387 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.
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: 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_1000186023
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)
	B2VFE0 [UniParc]. Last modified July 1, 2008. Version 1. Checksum: 20474CF494EDCF55	FASTA	387	40,871
	10 20 30 40 50 60 MEKVVIVDAI RTPMGRSKGG AFRHVRAEDL SAHLMRSLLS RNPSVDPATL DDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NAALLAEIPH SVPATTVNRL CGSSMQALHD AARAIMVGDA RTCLIGGVEH 130 140 150 160 170 180 MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDRFAA RSHQRAAAAT 190 200 210 220 230 240 QAGHFAAEIV AVCGHDADGV LKRYDADEVI RPETTVESLM ALRPAFDPVD GTVTAGSSSA 250 260 270 280 290 300 LSDGAAAMLI MSGSQARQQG LKARARIRSM AVVGCDPSIM GYGPVPASQL ALKRAGLSIA 310 320 330 340 350 360 DIGVFELNEA FAAQTLPCIK DLGLMDKLDE KVNLNGGAIA LGHPLGCSGA RISTTLLNLM 370 380 ERRDAQFGLA TMCIGLGQGI ATVFERI

References

[1]

"The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic bacterium in the genus Erwinia." Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., Geider K. Environ. Microbiol. 10:2211-2222(2008) [PubMed: 18462403] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 17950 / Et1/99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU468135 Genomic DNA. Translation: CAO95291.1.
RefSeq	YP_001906199.1. NC_010694.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6298942.
GenomeReviews	Gene locus ETA_02450 in contig CU468135_GR.
PATRIC	20426172. VBIErwTas9546_0291.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	AIDDIYW.
ProtClustDB	PRK08947.
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.
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_ERWT9

Accession

Primary (citable) accession number: B2VFE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	July 1, 2008
Last modified:	January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program