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Protein

Bile acid-CoA:amino acid N-acyltransferase

Gene

BAAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

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.

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)DescriptionActionsGraphical viewLength
Active sitei235Charge relay systemCurated1
Active sitei328Charge relay systemCurated1
Active sitei362Charge relay systemCurated1

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
  • myristoyl-CoA hydrolase activity Source: UniProtKB-EC
  • N-acyltransferase activity Source: MGI
  • palmitoyl-CoA hydrolase activity Source: UniProtKB-EC
  • signaling receptor binding Source: UniProtKB
  • transferase activity, transferring acyl groups Source: Reactome
  • very long chain acyl-CoA hydrolase activity Source: UniProtKB

GO - Biological processi

  • acyl-CoA metabolic process Source: UniProtKB
  • animal organ regeneration Source: Ensembl
  • bile acid biosynthetic process Source: UniProtKB
  • bile acid conjugation Source: UniProtKB
  • bile acid metabolic process Source: Reactome
  • fatty acid metabolic process Source: GO_Central
  • glycine metabolic process Source: UniProtKB
  • liver development Source: Ensembl
  • protein targeting to peroxisome Source: Reactome
  • taurine metabolic process Source: UniProtKB

Keywordsi

Molecular functionAcyltransferase, Hydrolase, Serine esterase, Transferase
Biological processFatty 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
R-HSA-9033241 Peroxisomal protein import
SABIO-RKiQ14032

Protein family/group databases

ESTHERihuman-BAAT Acyl-CoA_Thioesterase
MEROPSiS09.A50

Chemistry databases

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

EuPathDBiHostDB:ENSG00000136881.11
HGNCiHGNC:932 BAAT
MIMi602938 gene
neXtProtiNX_Q14032

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_02373776M → V in FHCA. 1 PublicationCorresponds to variant dbSNP:rs28937579EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi235C → A: Abolishes activity. 2 Publications1
Mutagenesisi235C → 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 Publications1
Mutagenesisi328D → A: Abolishes activity. 2 Publications1
Mutagenesisi362H → A: Abolishes activity. 2 Publications1
Mutagenesisi372C → A: Retains activity. 1
Mutagenesisi417Q → K: Translocation to peroxisomes. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi570
MalaCardsiBAAT
MIMi607748 phenotype
OpenTargetsiENSG00000136881
Orphaneti238475 Familial hypercholanemia
PharmGKBiPA25231

Chemistry databases

DrugBankiDB00145 Glycine
DB05990 Obeticholic acid

Polymorphism and mutation databases

BioMutaiBAAT
DMDMi74739811

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002021591 – 418Bile acid-CoA:amino acid N-acyltransferaseAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei125PhosphoserineBy similarity1
Modified residuei416PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14032
PaxDbiQ14032
PeptideAtlasiQ14032
PRIDEiQ14032
ProteomicsDBi59802

PTM databases

CarbonylDBiQ14032
iPTMnetiQ14032
PhosphoSitePlusiQ14032

Expressioni

Tissue specificityi

Expressed in liver, gallbladder mucosa and pancreas.2 Publications

Gene expression databases

BgeeiENSG00000136881
CleanExiHS_BAAT
GenevisibleiQ14032 HS

Organism-specific databases

HPAiHPA021251
HPA021330

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • signaling receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107046, 5 interactors
IntActiQ14032, 21 interactors
MINTiQ14032
STRINGi9606.ENSP00000259407

Structurei

3D structure databases

ProteinModelPortaliQ14032
SMRiQ14032
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
OMAiIPQVYRG
OrthoDBiEOG091G08KU
PhylomeDBiQ14032
TreeFamiTF314911

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR016662 Acyl-CoA_thioEstase_long-chain
IPR014940 BAAT_C
IPR006862 Thio_Ohase/aa_AcTrfase
PfamiView protein in Pfam
PF08840 BAAT_C, 1 hit
PF04775 Bile_Hydr_Trans, 1 hit
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05230320R → Q3 PublicationsCorresponds to variant dbSNP:rs1572983EnsemblClinVar.1
Natural variantiVAR_02373776M → V in FHCA. 1 PublicationCorresponds to variant dbSNP:rs28937579EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34081 mRNA Translation: AAC37550.1
CR541918 mRNA Translation: CAG46716.1
AL359893 Genomic DNA No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiBAAT_HUMAN
AccessioniPrimary (citable) accession number: Q14032
Secondary accession number(s): Q3B7W9, Q96L31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1996
Last modified: June 20, 2018
This is version 145 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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