Reviewed, UniProtKB/Swiss-Prot O32177 (FADA_BACSU)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase

Gene names

Name:	fadA
Synonyms:	yusK
Ordered Locus Names:	BSU32830

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in the degradation of long-chain fatty acids.
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Induction	Repressed by fadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize fadR as to its binding to fadR boxes on target DNA and thus derepress transcription. Ref.2
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
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
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 – 391	391	3-ketoacyl-CoA thiolase		PRO_0000360669
Sites
	Active site	90	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)
	O32177-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: B326A3D6A64E5799	FASTA	391	41,123
	10 20 30 40 50 60 MKEAVIVSGA RTPVGKAKKG SLATVRPDDL GAICVKETLK RAGGYEGNID DLIIGCATPE 70 80 90 100 110 120 AEQGLNMARN IGALAGLPYT VPAITVNRYC SSGLQSIAYA AEKIMLGAYD TAIAGGAESM 130 140 150 160 170 180 SQVPMMGHVT RPNLALAEKA PEYYMSMGHT AEQVAKKYGV SREDQDAFAV RSHQNAAKAL 190 200 210 220 230 240 AEGKFKDEIV PVEVTVTEIG EDHKPMEKQF VFSQDEGVRP QTTADILSTL RPAFSVDGTV 250 260 270 280 290 300 TAGNSSQTSD GAAAVMLMDR EKADALGLAP LVKFRSFAVG GVPPEVMGIG PVEAIPRALK 310 320 330 340 350 360 LAGLQLQDIG LFELNEAFAS QAIQVIRELG IDEEKVNVNG GAIALGHPLG CTGTKLTLSL 370 380 390 IHEMKRRNEQ FGVVTMCIGG GMGAAGVFEL C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation." Matsuoka H., Hirooka K., Fujita Y. J. Biol. Chem. 282:5180-5194(2007) [PubMed: 17189250] [Abstract] Cited for: GENE NAME, INDUCTION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB15272.1.
PIR	D70021.
RefSeq	NP_391162.1.
3D structure databases
HSSP	HSSP built from PDB template 1AFW based on UniProtKB P27796.
ModBase	Search...
Genome annotation databases
GeneID	936729.
GenomeReviews	Gene locus BSU32830 in contig AL009126_GR.
KEGG	bsu:BSU32830.
NMPDR	fig|224308.1.peg.3288.
Organism-specific databases
SubtiList	BG14023. fadA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O32177.
OMA	GCATPEA.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3279-MON.
Family and domain databases
InterPro	IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	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.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 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_BACSU

Accession

Primary (citable) accession number: O32177

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)