B5FEW7 (FADA_VIBFM) 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:	VFMJ11_0023

Organism

Vibrio fischeri (strain MJ11) [Complete proteome] [HAMAP]

Taxonomic identifier

388396 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio

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_1000186025
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)
	B5FEW7 [UniParc]. Last modified October 14, 2008. Version 1. Checksum: FF77F87E8A8867BB	FASTA	387	40,915
	10 20 30 40 50 60 MKNVVIVDCI RTPMGRSKNG VFRYTRAEDL SAHLMKGLLK RNPSVDPNDI EDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNIAR NSALLAGLPQ SIAATTVNRL CGSSMQALHD ASRAIMVGDA EICIIGGVEH 130 140 150 160 170 180 MGHVPMNHGV DFHSGLSKSV AKASGMMGLT AEMLGKMHGI SREQQDAFAL ASHQKAHKAT 190 200 210 220 230 240 IEGYFDSEIL PIEGHDENGV LTLVTHDEVI RPETTLEGLA ALRPAFDPAN GTVTAGSSSA 250 260 270 280 290 300 LSDGASAMLV MSEEKANELG LPIRAKVRSM AVSGCDPSIM GYGPVPATKK ALKRAGLSLD 310 320 330 340 350 360 DIELFELNEA FAAQSLPCIK DLGLLDVMDE KVNLNGGAIA LGHPLGCSGS RIATTLINNM 370 380 ERTGAKLGVA TMCIGLGQGI ATVFERP

References

[1]

"Complete sequence of Vibrio fischeri strain MJ11." Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MJ11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001139 Genomic DNA. Translation: ACH65092.1.
RefSeq	YP_002154795.1. NC_011184.1.
3D structure databases
ProteinModelPortal	B5FEW7.
SMR	B5FEW7. Positions 2-386.
ModBase	Search...
Protein-protein interaction databases
STRING	B5FEW7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6805191.
GenomeReviews	Gene locus VFMJ11_0023 in contig CP001139_GR.
KEGG	vfm:VFMJ11_0023.
PATRIC	20118499. VBIVibFis37164_0024.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG370930.
OMA	TNNGDVF.
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_VIBFM

Accession

Primary (citable) accession number: B5FEW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	October 14, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program