UniProt Accession

 BAAT_MOUSE; Q91X34; A2AKK7; O08833; Q8C1I3 

Genbank Protein ID

 U95215; AK017923; AL772310; CH466565; BC012683 

Genbank Nucleotide ID

 AAB58325.1; BAC25534.1; CAM21769.1; EDL02319.1 

Protein Name

 Bile acid-CoA:amino acid N-acyltransferase 

Protein Synonyms/Alias

 BACAT; BAT; Glycine N-choloyltransferase; Long-chain fatty-acyl-CoA hydrolase 

Gene Name

 Baat 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
40	QASLKDEKGNLFSSQ	acetylation	[1, 2, 3, 4, 5]
40	QASLKDEKGNLFSSQ	succinylation	[4]
40	QASLKDEKGNLFSSQ	ubiquitination	[6]
138	WYVAPGVKRIQVKES	acetylation	[3, 5]
138	WYVAPGVKRIQVKES	ubiquitination	[6]
305	TFQETADKDSKYCFP	acetylation	[1, 2, 5]
308	ETADKDSKYCFPIEK	acetylation	[2, 3, 5]
308	ETADKDSKYCFPIEK	ubiquitination	[6]
334	DDKNLNSKVHANQAI	ubiquitination	[6]
346	QAIAQLMKNGKKNWT	acetylation	[4]
346	QAIAQLMKNGKKNWT	succinylation	[4]
350	QLMKNGKKNWTLLSY	acetylation	[4]
350	QLMKNGKKNWTLLSY	succinylation	[4]
406	HSWKEIQKFLKQHLL	acetylation	[2, 3, 5]
409	KEIQKFLKQHLLPDL	acetylation	[4]
409	KEIQKFLKQHLLPDL	succinylation	[4]
409	KEIQKFLKQHLLPDL	ubiquitination	[6]

Reference

 [1] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity). 

Sequence Annotation

 ACT_SITE 235 235 Charge relay system (By similarity).
 ACT_SITE 328 328 Charge relay system (By similarity).
 ACT_SITE 362 362 Charge relay system (By similarity).  

Keyword

 Acyltransferase; Complete proteome; Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism; Peroxisome; Reference proteome; Serine esterase; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 420 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
 GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
 GO:0047963; F:glycine N-choloyltransferase activity; IEA:EC.
 GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IEA:Compara.
 GO:0016410; F:N-acyltransferase activity; IDA:MGI.
 GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:EC.
 GO:0052817; F:very long chain acyl-CoA hydrolase activity; IEA:Compara.
 GO:0006637; P:acyl-CoA metabolic process; IEA:Compara.
 GO:0006699; P:bile acid biosynthetic process; IEA:Compara.
 GO:0002152; P:bile acid conjugation; IEA:Compara.
 GO:0008206; P:bile acid metabolic process; IDA:MGI.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
 GO:0006544; P:glycine metabolic process; IEA:Compara.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0031100; P:organ regeneration; IEA:Compara.
 GO:0019530; P:taurine metabolic process; IEA:Compara. 

Interpro

 IPR016662; Acyl-CoA_thioEstase_long-chain.
 IPR014940; BAAT_C.
 IPR006862; Thio_Ohase/aa_AcTrfase. 

Pfam

 PF08840; BAAT_C
 PF04775; Bile_Hydr_Trans 

SMART

  

PROSITE

  

PRINTS