BAAT_HUMAN
ID BAAT_HUMAN Reviewed; 418 AA.
AC Q14032; Q3B7W9; Q96L31;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Bile acid-CoA:amino acid N-acyltransferase {ECO:0000303|PubMed:8034703};
DE Short=BACAT {ECO:0000303|PubMed:12810727};
DE Short=BAT {ECO:0000303|PubMed:8034703};
DE EC=2.3.1.65 {ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576, ECO:0000269|PubMed:8034703};
DE AltName: Full=Bile acid-CoA thioesterase {ECO:0000303|PubMed:12239217, ECO:0000303|PubMed:12810727};
DE AltName: Full=Choloyl-CoA hydrolase;
DE EC=3.1.2.27 {ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:8034703};
DE AltName: Full=Glycine N-choloyltransferase;
DE AltName: Full=Long-chain fatty-acyl-CoA hydrolase {ECO:0000303|PubMed:12810727};
DE EC=3.1.2.2 {ECO:0000269|PubMed:12810727};
GN Name=BAAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-17, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8034703; DOI=10.1016/s0021-9258(17)32178-6;
RA Falany C.N., Johnson M.R., Barnes S., Diasio R.B.;
RT "Glycine and taurine conjugation of bile acids by a single enzyme.
RT Molecular cloning and expression of human liver bile acid CoA:amino acid N-
RT acyltransferase.";
RL J. Biol. Chem. 269:19375-19379(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-20.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-20.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-20.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=2037576; DOI=10.1016/s0021-9258(18)99213-6;
RA Johnson M.R., Barnes S., Kwakye J.B., Diasio R.B.;
RT "Purification and characterization of bile acid-CoA:amino acid N-
RT acyltransferase from human liver.";
RL J. Biol. Chem. 266:10227-10233(1991).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-235; ASP-328 AND HIS-362,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12239217; DOI=10.1074/jbc.m207463200;
RA Sfakianos M.K., Wilson L., Sakalian M., Falany C.N., Barnes S.;
RT "Conserved residues in the putative catalytic triad of human bile acid
RT Coenzyme A:amino acid N-acyltransferase.";
RL J. Biol. Chem. 277:47270-47275(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF CYS-235; ASP-328; HIS-362; CYS-372 AND GLN-417, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12810727; DOI=10.1074/jbc.m300987200;
RA O'Byrne J., Hunt M.C., Rai D.K., Saeki M., Alexson S.E.;
RT "The human bile acid-CoA:amino acid N-acyltransferase functions in the
RT conjugation of fatty acids to glycine.";
RL J. Biol. Chem. 278:34237-34244(2003).
RN [9]
RP INVOLVEMENT IN BACD1, VARIANTS BACD1 20-ARG--LEU-418 DEL; VAL-69; THR-84
RP AND ARG-386, CHARACTERIZATION OF VARIANTS BACD1 20-ARG--LEU-418 DEL; VAL-69
RP AND ARG-386, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23415802; DOI=10.1053/j.gastro.2013.02.004;
RA Setchell K.D., Heubi J.E., Shah S., Lavine J.E., Suskind D., Al-Edreesi M.,
RA Potter C., Russell D.W., O'Connell N.C., Wolfe B., Jha P., Zhang W.,
RA Bove K.E., Knisely A.S., Hofmann A.F., Rosenthal P., Bull L.N.;
RT "Genetic defects in bile acid conjugation cause fat-soluble vitamin
RT deficiency.";
RL Gastroenterology 144:945-955(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP INVOLVEMENT IN BACD1, AND VARIANT BACD1 VAL-76.
RX PubMed=12704386; DOI=10.1038/ng1147;
RA Carlton V.E.H., Harris B.Z., Puffenberger E.G., Batta A.K., Knisely A.S.,
RA Robinson D.L., Strauss K.A., Shneider B.L., Lim W.A., Salen G.,
RA Morton D.H., Bull L.N.;
RT "Complex inheritance of familial hypercholanemia with associated mutations
RT in TJP2 and BAAT.";
RL Nat. Genet. 34:91-96(2003).
CC -!- FUNCTION: Catalyzes the amidation of bile acids (BAs) with the amino
CC acids taurine and glycine (PubMed:12810727, PubMed:8034703,
CC PubMed:2037576, PubMed:12239217). More than 95% of the BAs are N-acyl
CC amidates with glycine and taurine (PubMed:8034703). Amidation of BAs in
CC the liver with glycine or taurine prior to their excretion into bile is
CC an important biochemical event in bile acid metabolism
CC (PubMed:12810727). This conjugation (or amidation) plays several
CC important biological roles in that it promotes the secretion of BAs and
CC cholesterol into bile and increases the detergent properties of BAs in
CC the intestine, which facilitates lipid and vitamin absorption
CC (PubMed:12810727). May also act as an acyl-CoA thioesterase that
CC regulates intracellular levels of free fatty acids (PubMed:12810727,
CC PubMed:8034703, PubMed:12239217). In vitro, catalyzes the hydrolysis of
CC long- and very long-chain saturated acyl-CoAs to the free fatty acid
CC and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs
CC (PubMed:12810727). {ECO:0000269|PubMed:12239217,
CC ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576,
CC ECO:0000269|PubMed:8034703, ECO:0000303|PubMed:12810727,
CC ECO:0000303|PubMed:8034703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + glycine = CoA + glycocholate + H(+);
CC Xref=Rhea:RHEA:14001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57373; EC=2.3.1.65;
CC Evidence={ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727,
CC ECO:0000269|PubMed:2037576, ECO:0000269|PubMed:8034703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14002;
CC Evidence={ECO:0000305|PubMed:12239217, ECO:0000305|PubMed:12810727,
CC ECO:0000305|PubMed:2037576, ECO:0000305|PubMed:8034703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
CC Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27;
CC Evidence={ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727,
CC ECO:0000269|PubMed:8034703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
CC Evidence={ECO:0000305|PubMed:12239217, ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+);
CC Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
CC Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
CC Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
CC Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + taurine = CoA + H(+) + taurocholate;
CC Xref=Rhea:RHEA:47100, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:8034703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47101;
CC Evidence={ECO:0000305|PubMed:12810727, ECO:0000305|PubMed:8034703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + glycine = CoA + glycochenodeoxycholate
CC + H(+); Xref=Rhea:RHEA:49788, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:62989;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49789;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + taurine = CoA + H(+) +
CC taurochenodeoxycholate; Xref=Rhea:RHEA:49784, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49785;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + glycine = CoA + H(+) + N-eicosanoylglycinate;
CC Xref=Rhea:RHEA:49792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57380, ChEBI:CHEBI:87391;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49793;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + hexacosanoyl-CoA = CoA + H(+) + N-
CC hexacosanoylglycine; Xref=Rhea:RHEA:49772, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:64868,
CC ChEBI:CHEBI:87414; Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49773;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + glycine = CoA + H(+) + N-docosanoylglycine;
CC Xref=Rhea:RHEA:49780, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:65059, ChEBI:CHEBI:87410;
CC Evidence={ECO:0000269|PubMed:12810727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49781;
CC Evidence={ECO:0000305|PubMed:12810727};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for taurine toward choloyl-CoA
CC {ECO:0000269|PubMed:2037576};
CC KM=1.8 mM for taurine toward choloyl-CoA
CC {ECO:0000269|PubMed:8034703};
CC KM=5.6 mM for glycine toward choloyl-CoA
CC {ECO:0000269|PubMed:8034703};
CC KM=5.8 mM for glycine toward choloyl-CoA
CC {ECO:0000269|PubMed:2037576};
CC KM=2.2 mM for 2-fluoro-beta-alanine toward choloyl-CoA
CC {ECO:0000269|PubMed:2037576};
CC KM=19.3 uM for glycine toward arachidoyl-CoA
CC {ECO:0000269|PubMed:12810727};
CC KM=50.02 uM for choloyl-CoA (acyl-CoA thioesterase activity)
CC {ECO:0000269|PubMed:12239217};
CC Vmax=0.33 umol/min/mg enzyme with taurine as substrate for
CC acyltransferase activity {ECO:0000269|PubMed:2037576};
CC Vmax=0.19 umol/min/mg enzyme with 2-fluoro-beta-alanine as substrate
CC for acyltransferase activity {ECO:0000269|PubMed:2037576};
CC Vmax=0.77 umol/min/mg enzyme with glycine as substrate for
CC acyltransferase activity {ECO:0000269|PubMed:2037576};
CC Vmax=223 nmol/min/mg enzyme with arachidoyl-CoA as substrate for
CC acyl-CoA thioesterase activity {ECO:0000269|PubMed:12810727};
CC Vmax=1.48 umol/min/ug enzyme for acyl-CoA thioesterase activity
CC {ECO:0000269|PubMed:12239217};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2037576}.
CC -!- INTERACTION:
CC Q14032; P55212: CASP6; NbExp=3; IntAct=EBI-8994378, EBI-718729;
CC Q14032; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-8994378, EBI-10181276;
CC Q14032; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-8994378, EBI-10181260;
CC Q14032; O00291: HIP1; NbExp=3; IntAct=EBI-8994378, EBI-473886;
CC Q14032; P30519: HMOX2; NbExp=3; IntAct=EBI-8994378, EBI-712096;
CC Q14032; Q92993: KAT5; NbExp=3; IntAct=EBI-8994378, EBI-399080;
CC Q14032; P13473-2: LAMP2; NbExp=3; IntAct=EBI-8994378, EBI-21591415;
CC Q14032; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-8994378, EBI-11742507;
CC Q14032; P62937-2: PPIA; NbExp=3; IntAct=EBI-8994378, EBI-25884072;
CC Q14032; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-8994378, EBI-5280197;
CC Q14032; P62826: RAN; NbExp=3; IntAct=EBI-8994378, EBI-286642;
CC Q14032; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-8994378, EBI-9090795;
CC Q14032; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-8994378, EBI-2623095;
CC Q14032; P61981: YWHAG; NbExp=3; IntAct=EBI-8994378, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12810727,
CC ECO:0000269|PubMed:23415802, ECO:0000269|PubMed:8034703}. Peroxisome
CC {ECO:0000250|UniProtKB:Q63276}.
CC -!- TISSUE SPECIFICITY: Expressed in the gallbladder mucosa and pancreas
CC (PubMed:2037576, PubMed:12810727). Expressed in hepatocytes (at protein
CC level) (PubMed:2037576, PubMed:12810727, PubMed:23415802).
CC {ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576,
CC ECO:0000269|PubMed:23415802}.
CC -!- DISEASE: Bile acid conjugation defect 1 (BACD1) [MIM:619232]: An
CC autosomal recessive metabolic disorder characterized by reduced biliary
CC secretion of conjugated bile acids, fat malabsorption, and fat-soluble
CC vitamin deficiency. Clinical manifestations include rickets with
CC variable growth failure due to vitamin D deficiency, and coagulopathy
CC due to deficiency of vitamin K-dependent clotting factors. Additional
CC variable features include pruritis, anemia, hepatomegaly, and bile duct
CC proliferation on liver biopsy. Laboratory studies show abnormally
CC increased levels of unconjugated bile acids.
CC {ECO:0000269|PubMed:12704386, ECO:0000269|PubMed:23415802}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; L34081; AAC37550.1; -; mRNA.
DR EMBL; CR541918; CAG46716.1; -; mRNA.
DR EMBL; AL359893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58943.1; -; Genomic_DNA.
DR EMBL; BC009567; AAH09567.1; -; mRNA.
DR EMBL; BC107424; AAI07425.1; -; mRNA.
DR CCDS; CCDS6752.1; -.
DR PIR; A53965; A53965.
DR RefSeq; NP_001121082.1; NM_001127610.1.
DR RefSeq; NP_001692.1; NM_001701.3.
DR AlphaFoldDB; Q14032; -.
DR SMR; Q14032; -.
DR BioGRID; 107046; 34.
DR IntAct; Q14032; 36.
DR MINT; Q14032; -.
DR STRING; 9606.ENSP00000259407; -.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB01956; Taurine.
DR SwissLipids; SLP:000001309; -.
DR ESTHER; human-BAAT; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A50; -.
DR CarbonylDB; Q14032; -.
DR iPTMnet; Q14032; -.
DR PhosphoSitePlus; Q14032; -.
DR BioMuta; BAAT; -.
DR DMDM; 74739811; -.
DR MassIVE; Q14032; -.
DR MaxQB; Q14032; -.
DR PaxDb; Q14032; -.
DR PeptideAtlas; Q14032; -.
DR PRIDE; Q14032; -.
DR ProteomicsDB; 59802; -.
DR Antibodypedia; 14641; 215 antibodies from 29 providers.
DR DNASU; 570; -.
DR Ensembl; ENST00000259407.7; ENSP00000259407.2; ENSG00000136881.12.
DR Ensembl; ENST00000395051.4; ENSP00000378491.3; ENSG00000136881.12.
DR Ensembl; ENST00000621712.2; ENSP00000484063.1; ENSG00000276559.2.
DR Ensembl; ENST00000674556.1; ENSP00000501610.1; ENSG00000136881.12.
DR GeneID; 570; -.
DR KEGG; hsa:570; -.
DR MANE-Select; ENST00000259407.7; ENSP00000259407.2; NM_001701.4; NP_001692.1.
DR UCSC; uc010mtd.3; human.
DR CTD; 570; -.
DR DisGeNET; 570; -.
DR GeneCards; BAAT; -.
DR HGNC; HGNC:932; BAAT.
DR HPA; ENSG00000136881; Tissue enriched (liver).
DR MalaCards; BAAT; -.
DR MIM; 602938; gene.
DR MIM; 619232; phenotype.
DR neXtProt; NX_Q14032; -.
DR OpenTargets; ENSG00000136881; -.
DR Orphanet; 238475; Familial hypercholanemia.
DR PharmGKB; PA25231; -.
DR VEuPathDB; HostDB:ENSG00000136881; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q14032; -.
DR OMA; LTPFQVV; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q14032; -.
DR TreeFam; TF314911; -.
DR BRENDA; 2.3.1.65; 2681.
DR PathwayCommons; Q14032; -.
DR Reactome; R-HSA-159418; Recycling of bile acids and salts.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; Q14032; -.
DR SignaLink; Q14032; -.
DR BioGRID-ORCS; 570; 8 hits in 1065 CRISPR screens.
DR GeneWiki; BAAT; -.
DR GenomeRNAi; 570; -.
DR Pharos; Q14032; Tbio.
DR PRO; PR:Q14032; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q14032; protein.
DR Bgee; ENSG00000136881; Expressed in liver and 85 other tissues.
DR ExpressionAtlas; Q14032; baseline and differential.
DR Genevisible; Q14032; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; TAS:Reactome.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047963; F:glycine N-choloyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:MGI.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052817; F:very long chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0002152; P:bile acid conjugation; IDA:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; TAS:Reactome.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0019530; P:taurine metabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Direct protein sequencing; Disease variant;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Peroxisome;
KW Phosphoprotein; Reference proteome; Serine esterase; Transferase.
FT CHAIN 1..418
FT /note="Bile acid-CoA:amino acid N-acyltransferase"
FT /id="PRO_0000202159"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 362
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63276"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63276"
FT VARIANT 20..418
FT /note="Missing (in BACD1; contrary to wild-type,
FT undetectable expression in hepatocytes)"
FT /evidence="ECO:0000269|PubMed:23415802"
FT /id="VAR_085492"
FT VARIANT 20
FT /note="R -> Q (in dbSNP:rs1572983)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_052303"
FT VARIANT 69
FT /note="D -> V (in BACD1; unknown pathological significance;
FT contrary to wild-type, undetectable expression in
FT hepatocytes)"
FT /evidence="ECO:0000269|PubMed:23415802"
FT /id="VAR_085493"
FT VARIANT 76
FT /note="M -> V (in BACD1; dbSNP:rs28937579)"
FT /evidence="ECO:0000269|PubMed:12704386"
FT /id="VAR_023737"
FT VARIANT 84
FT /note="P -> T (in BACD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23415802"
FT /id="VAR_085494"
FT VARIANT 386
FT /note="G -> R (in BACD1; unknown pathological significance;
FT contrary to wild-type, undetectable expression in
FT hepatocytes)"
FT /evidence="ECO:0000269|PubMed:23415802"
FT /id="VAR_085495"
FT MUTAGEN 235
FT /note="C->A: Abolishes N-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12239217,
FT ECO:0000269|PubMed:12810727"
FT MUTAGEN 235
FT /note="C->S: Lowers N-acyltransferase activity; enhanced
FT thioesterase activity presumably dependent on the formation
FT of a bile acid-enzyme covalent intermediate via a thioester
FT bond."
FT /evidence="ECO:0000269|PubMed:12239217,
FT ECO:0000269|PubMed:12810727"
FT MUTAGEN 328
FT /note="D->A: Abolishes N-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12239217,
FT ECO:0000269|PubMed:12810727"
FT MUTAGEN 362
FT /note="H->A: Abolishes N-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12239217"
FT MUTAGEN 362
FT /note="H->Q: Abolishes N-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12810727"
FT MUTAGEN 372
FT /note="C->A: Retains N-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12810727"
FT MUTAGEN 417
FT /note="Q->K: Translocation to peroxisomes."
FT /evidence="ECO:0000269|PubMed:12810727"
SQ SEQUENCE 418 AA; 46299 MW; 4B290BAEE97F23B3 CRC64;
MIQLTATPVS ALVDEPVHIR ATGLIPFQMV SFQASLEDEN GDMFYSQAHY RANEFGEVDL
NHASSLGGDY MGVHPMGLFW SLKPEKLLTR LLKRDVMNRP FQVQVKLYDL ELIVNNKVAS
APKASLTLER WYVAPGVTRI KVREGRLRGA LFLPPGEGLF PGVIDLFGGL GGLLEFRASL
LASRGFASLA LAYHNYEDLP RKPEVTDLEY FEEAANFLLR HPKVFGSGVG VVSVCQGVQI
GLSMAIYLKQ VTATVLINGT NFPFGIPQVY HGQIHQPLPH SAQLISTNAL GLLELYRTFE
TTQVGASQYL FPIEEAQGQF LFIVGEGDKT INSKAHAEQA IGQLKRHGKN NWTLLSYPGA
GHLIEPPYSP LCCASTTHDL RLHWGGEVIP HAAAQEHAWK EIQRFLRKHL IPDVTSQL
