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Protein

Bile acid-CoA:amino acid N-acyltransferase

Gene

BAAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and 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.2 Publications

Catalytic activityi

Choloyl-CoA + glycine = CoA + glycocholate.2 Publications
Palmitoyl-CoA + H2O = CoA + palmitate.1 Publication

Kineticsi

  1. KM=1.1 mM for taurine toward choloyl-CoA2 Publications
  2. KM=2.2 mM for 2-fluoro-beta-alanine toward choloyl-CoA2 Publications
  3. KM=5.8 mM for glycine toward choloyl-CoA2 Publications
  4. KM=19.3 µM for arachidoyl-CoA1 Publication
  1. Vmax=0.33 µmol/min/mg enzyme with taurine as substrate for acyltransferase activity2 Publications
  2. Vmax=0.19 µmol/min/mg enzyme with 2-fluoro-beta-alanine as substrate for acyltransferase activity1 Publication
  3. Vmax=0.77 µmol/min/mg enzyme with glycine as substrate for acyltransferase activity2 Publications
  4. Vmax=223 nmol/min/mg enzyme with arachidoyl-CoA as substrate for acyl-CoA thioesterase activity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei235 – 2351Charge relay systemCurated
Active sitei328 – 3281Charge relay systemCurated
Active sitei362 – 3621Charge relay systemCurated

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: UniProtKB-KW
  • glycine N-choloyltransferase activity Source: UniProtKB
  • long-chain acyl-CoA hydrolase activity Source: UniProtKB
  • medium-chain acyl-CoA hydrolase activity Source: UniProtKB
  • N-acyltransferase activity Source: MGI
  • palmitoyl-CoA hydrolase activity Source: UniProtKB-EC
  • receptor binding Source: UniProtKB
  • very long chain acyl-CoA hydrolase activity Source: UniProtKB

GO - Biological processi

  • acyl-CoA metabolic process Source: UniProtKB
  • bile acid and bile salt transport Source: Reactome
  • bile acid biosynthetic process Source: UniProtKB
  • bile acid conjugation Source: UniProtKB
  • bile acid metabolic process Source: Reactome
  • fatty acid metabolic process Source: UniProtKB-KW
  • glycine metabolic process Source: UniProtKB
  • liver development Source: Ensembl
  • organ regeneration Source: Ensembl
  • small molecule metabolic process Source: Reactome
  • taurine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Serine esterase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.65. 2681.
ReactomeiR-HSA-159418. Recycling of bile acids and salts.
R-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
SABIO-RKQ14032.

Protein family/group databases

ESTHERihuman-BAAT. Acyl-CoA_Thioesterase.
MEROPSiS09.A50.

Chemistry

SwissLipidsiSLP:000001309.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile acid-CoA:amino acid N-acyltransferase1 Publication (EC:2.3.1.652 Publications)
Short name:
BACAT1 Publication
Short name:
BAT1 Publication
Alternative name(s):
Glycine N-choloyltransferase
Long-chain fatty-acyl-CoA hydrolase1 Publication (EC:3.1.2.21 Publication)
Gene namesi
Name:BAAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:932. BAAT.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Familial hypercholanemia (FHCA)1 Publication
The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
Disease descriptionA disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.
See also OMIM:607748
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761M → V in FHCA. 1 Publication
Corresponds to variant rs28937579 [ dbSNP | Ensembl ].
VAR_023737

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2351C → A: Abolishes activity. 2 Publications
Mutagenesisi235 – 2351C → S: Lowers N-acyltransferase activity; enhanced thioesterase activity presumably dependent on the formation of a bile acid-enzyme covalent intermediate via a thioester bond. 2 Publications
Mutagenesisi328 – 3281D → A: Abolishes activity. 2 Publications
Mutagenesisi362 – 3621H → A: Abolishes activity. 2 Publications
Mutagenesisi372 – 3721C → A: Retains activity.
Mutagenesisi417 – 4171Q → K: Translocation to peroxisomes. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiBAAT.
MIMi607748. phenotype.
Orphaneti238475. Familial hypercholanemia.
PharmGKBiPA25231.

Chemistry

DrugBankiDB00145. Glycine.

Polymorphism and mutation databases

BioMutaiBAAT.
DMDMi74739811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Bile acid-CoA:amino acid N-acyltransferasePRO_0000202159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251PhosphoserineBy similarity
Modified residuei416 – 4161PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14032.
PaxDbiQ14032.
PRIDEiQ14032.

PTM databases

iPTMnetiQ14032.
PhosphoSiteiQ14032.

Expressioni

Tissue specificityi

Expressed in liver, gallbladder mucosa and pancreas.2 Publications

Gene expression databases

BgeeiQ14032.
CleanExiHS_BAAT.
GenevisibleiQ14032. HS.

Organism-specific databases

HPAiHPA021251.
HPA021330.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA8DPQ0D2H93EBI-8994378,EBI-10181276
GOLGA8GQ08AF83EBI-8994378,EBI-10181260

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107046. 5 interactions.
IntActiQ14032. 21 interactions.
STRINGi9606.ENSP00000259407.

Structurei

3D structure databases

ProteinModelPortaliQ14032.
SMRiQ14032. Positions 14-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ14032.
KOiK00659.
OMAiAKPEVTD.
OrthoDBiEOG75TMC9.
PhylomeDBiQ14032.
TreeFamiTF314911.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 3 hits.

Sequencei

Sequence statusi: Complete.

Q14032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQLTATPVS ALVDEPVHIR ATGLIPFQMV SFQASLEDEN GDMFYSQAHY
60 70 80 90 100
RANEFGEVDL NHASSLGGDY MGVHPMGLFW SLKPEKLLTR LLKRDVMNRP
110 120 130 140 150
FQVQVKLYDL ELIVNNKVAS APKASLTLER WYVAPGVTRI KVREGRLRGA
160 170 180 190 200
LFLPPGEGLF PGVIDLFGGL GGLLEFRASL LASRGFASLA LAYHNYEDLP
210 220 230 240 250
RKPEVTDLEY FEEAANFLLR HPKVFGSGVG VVSVCQGVQI GLSMAIYLKQ
260 270 280 290 300
VTATVLINGT NFPFGIPQVY HGQIHQPLPH SAQLISTNAL GLLELYRTFE
310 320 330 340 350
TTQVGASQYL FPIEEAQGQF LFIVGEGDKT INSKAHAEQA IGQLKRHGKN
360 370 380 390 400
NWTLLSYPGA GHLIEPPYSP LCCASTTHDL RLHWGGEVIP HAAAQEHAWK
410
EIQRFLRKHL IPDVTSQL
Length:418
Mass (Da):46,299
Last modified:November 1, 1996 - v1
Checksum:i4B290BAEE97F23B3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → Q.3 Publications
Corresponds to variant rs1572983 [ dbSNP | Ensembl ].
VAR_052303
Natural varianti76 – 761M → V in FHCA. 1 Publication
Corresponds to variant rs28937579 [ dbSNP | Ensembl ].
VAR_023737

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34081 mRNA. Translation: AAC37550.1.
CR541918 mRNA. Translation: CAG46716.1.
AL359893 Genomic DNA. Translation: CAH72995.1.
CH471105 Genomic DNA. Translation: EAW58943.1.
BC009567 mRNA. Translation: AAH09567.1.
BC107424 mRNA. Translation: AAI07425.1.
CCDSiCCDS6752.1.
PIRiA53965.
RefSeqiNP_001121082.1. NM_001127610.1.
NP_001692.1. NM_001701.3.
UniGeneiHs.284712.

Genome annotation databases

EnsembliENST00000259407; ENSP00000259407; ENSG00000136881.
ENST00000395051; ENSP00000378491; ENSG00000136881.
ENST00000621712; ENSP00000484063; ENSG00000276559.
GeneIDi570.
KEGGihsa:570.
UCSCiuc010mtd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34081 mRNA. Translation: AAC37550.1.
CR541918 mRNA. Translation: CAG46716.1.
AL359893 Genomic DNA. Translation: CAH72995.1.
CH471105 Genomic DNA. Translation: EAW58943.1.
BC009567 mRNA. Translation: AAH09567.1.
BC107424 mRNA. Translation: AAI07425.1.
CCDSiCCDS6752.1.
PIRiA53965.
RefSeqiNP_001121082.1. NM_001127610.1.
NP_001692.1. NM_001701.3.
UniGeneiHs.284712.

3D structure databases

ProteinModelPortaliQ14032.
SMRiQ14032. Positions 14-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107046. 5 interactions.
IntActiQ14032. 21 interactions.
STRINGi9606.ENSP00000259407.

Chemistry

DrugBankiDB00145. Glycine.
SwissLipidsiSLP:000001309.

Protein family/group databases

ESTHERihuman-BAAT. Acyl-CoA_Thioesterase.
MEROPSiS09.A50.

PTM databases

iPTMnetiQ14032.
PhosphoSiteiQ14032.

Polymorphism and mutation databases

BioMutaiBAAT.
DMDMi74739811.

Proteomic databases

MaxQBiQ14032.
PaxDbiQ14032.
PRIDEiQ14032.

Protocols and materials databases

DNASUi570.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259407; ENSP00000259407; ENSG00000136881.
ENST00000395051; ENSP00000378491; ENSG00000136881.
ENST00000621712; ENSP00000484063; ENSG00000276559.
GeneIDi570.
KEGGihsa:570.
UCSCiuc010mtd.3. human.

Organism-specific databases

CTDi570.
GeneCardsiBAAT.
HGNCiHGNC:932. BAAT.
HPAiHPA021251.
HPA021330.
MalaCardsiBAAT.
MIMi602938. gene.
607748. phenotype.
neXtProtiNX_Q14032.
Orphaneti238475. Familial hypercholanemia.
PharmGKBiPA25231.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410II3X. Eukaryota.
COG1073. LUCA.
GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiQ14032.
KOiK00659.
OMAiAKPEVTD.
OrthoDBiEOG75TMC9.
PhylomeDBiQ14032.
TreeFamiTF314911.

Enzyme and pathway databases

BRENDAi2.3.1.65. 2681.
ReactomeiR-HSA-159418. Recycling of bile acids and salts.
R-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
SABIO-RKQ14032.

Miscellaneous databases

GeneWikiiBAAT.
GenomeRNAii570.
NextBioi2319.
PROiQ14032.
SOURCEiSearch...

Gene expression databases

BgeeiQ14032.
CleanExiHS_BAAT.
GenevisibleiQ14032. HS.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase."
    Falany C.N., Johnson M.R., Barnes S., Diasio R.B.
    J. Biol. Chem. 269:19375-19379(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-17, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Liver.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-20.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-20.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-20.
    Tissue: Liver.
  6. "Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver."
    Johnson M.R., Barnes S., Kwakye J.B., Diasio R.B.
    J. Biol. Chem. 266:10227-10233(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Liver.
  7. "Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase."
    Sfakianos M.K., Wilson L., Sakalian M., Falany C.N., Barnes S.
    J. Biol. Chem. 277:47270-47275(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-235; ASP-328 AND HIS-362.
  8. "The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine."
    O'Byrne J., Hunt M.C., Rai D.K., Saeki M., Alexson S.E.
    J. Biol. Chem. 278:34237-34244(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-235; ASP-328; HIS-362 AND GLN-417.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: VARIANT FHCA VAL-76.

Entry informationi

Entry nameiBAAT_HUMAN
AccessioniPrimary (citable) accession number: Q14032
Secondary accession number(s): Q3B7W9, Q96L31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In human, more than 95% of the biliary bile acids are N-acyl amidates with glycine and taurine. In other mammalian species large differences are observed in the relative amounts of taurine- and glycine-conjugated bile acids formed in bile.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.