Q1QUW9 (FADA_CHRSD) 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:	Csal_2392

Organism

Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]

Taxonomic identifier

290398 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Halomonadaceae › Chromohalobacter

Protein attributes

Sequence length	392 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 – 392	392	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000292887
Sites
	Active site	95	1	Acyl-thioester intermediate By similarity
	Active site	347	1	Proton acceptor By similarity
	Active site	377	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1QUW9 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: CC657D205AE37DDF	FASTA	392	41,321
	10 20 30 40 50 60 MSLNPRDIVV VDAVRTAMAK AKHGAFRNVR AENLSAAVMQ ALFDRNANLV PAEVDDVIWG 70 80 90 100 110 120 CVNQTLEQSM NIARNAAIMT GIPRTVPAQT VNRLCGSSMS ALHIATANIK AGMGDFYIIG 130 140 150 160 170 180 GVEHMEHVPM THGVDVNPAA SKYAAKAAMM MGLTAELLGK MHGVGREEQD AFGVRSHQRA 190 200 210 220 230 240 QAANENGYFD NEIVGVEGHD ADGFLRLIDR DEVIRQDANL EDMGKLKPVF DPKGGTVTAG 250 260 270 280 290 300 TSSALSVGAS ALAVMSYERA QALGLEPLAR VVSTGVAGCD ASIMGYGPVP ATQKALKSAG 310 320 330 340 350 360 LAIDDIQTVE LNEAFAAQSI PVLKDLGLRE RMDDAVNLHG GAIALGHPLG CSGARICTTL 370 380 390 LNVMRQQDTT LGLATMCIGM GQGVATVFER LK

References

[1]

"Complete sequence of Chromohalobacter salexigens DSM 3043." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 3043 / ATCC BAA-138 / NCIMB 13768.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000285 Genomic DNA. Translation: ABE59739.1.
RefSeq	YP_574438.1. NC_007963.1.
3D structure databases
ProteinModelPortal	Q1QUW9.
SMR	Q1QUW9. Positions 2-391.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1QUW9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4026829.
GenomeReviews	Gene locus Csal_2392 in contig CP000285_GR.
KEGG	csa:Csal_2392.
NMPDR	fig|290398.4.peg.2533.
PATRIC	21448614. VBIChrSal113723_2400.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0183.
HOGENOM	HBG370930.
OMA	SGARICT.
ProtClustDB	PRK08947.
Enzyme and pathway databases
BioCyc	CSAL290398:CSAL_2392-MONOMER.
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_CHRSD

Accession

Primary (citable) accession number: Q1QUW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program