A3M1H9 (FADA_ACIBT) 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:	A1S_0305

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length	390 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 – 390	390	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000292883
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	346	1	Proton acceptor By similarity
	Active site	376	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3M1H9 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: A59F51928FC3ED8B	FASTA	390	41,132
	10 20 30 40 50 60 MATLNPRDVV IVDGVRSAMG KSKNGMFRNV RADSLSAELV RALIARNQFD VNEVEDLIWG 70 80 90 100 110 120 CVNQTLEQGM NIGRNIGLLA GLPKTVAGQT VNRLCGSSMQ AIHTAAAQIA TNQGDIFIIG 130 140 150 160 170 180 GVEHMGHVGM MHGIDLNPEA SKHYAKASNM MGLTAEMLGR MNGITREEQD TFGVESHRRA 190 200 210 220 230 240 WAATQEGRFK NEIIGVEGHD ANGFKILCDI DEVIRPDANL EAFKALKPVF DPKGGSVTAA 250 260 270 280 290 300 TSSALSDGAS AMLLMSAERA QALGLKPRAV IRSMAVAGCD AAIMGYGPVP ATQKALKRAG 310 320 330 340 350 360 LSIADIQTVE LNEAFAAQGL SVLKGLGLYD KQDIVNLNGG AIALGHPLGC SGARITTTLL 370 380 390 NVMEQQDTQI GLATMCIGLG QGIATVIERV

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000521 Genomic DNA. Translation: ABO10773.2.
RefSeq	YP_001083375.1. NC_009085.1.
3D structure databases
ProteinModelPortal	A3M1H9.
SMR	A3M1H9. Positions 3-390.
ModBase	Search...
Protein-protein interaction databases
STRING	A3M1H9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4920251.
GenomeReviews	Gene locus A1S_0305 in contig CP000521_GR.
KEGG	acb:A1S_0305.
NMPDR	fig|400667.4.peg.313.
PATRIC	20716736. VBIAciBau103176_0307.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
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.
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_ACIBT

Accession

Primary (citable) accession number: A3M1H9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	December 14, 2011
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program