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Protein

Bile acid-CoA:amino acid N-acyltransferase

Gene

Baat

Organism
Rattus norvegicus (Rat)
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.By similarity

Catalytic activityi

Choloyl-CoA + glycine = CoA + glycocholate.2 Publications
Palmitoyl-CoA + H2O = CoA + palmitate.By similarity

Kineticsi

  1. KM=2.0 mM for taurine toward choloyl-CoA1 Publication
  2. KM=4.4 mM for glycine toward choloyl-CoA1 Publication

    Sites

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

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Hydrolase, Serine esterase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14337.
    ReactomeiR-RNO-159418. Recycling of bile acids and salts.
    R-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    SABIO-RKQ63276.

    Protein family/group databases

    ESTHERiratno-BAAT. Acyl-CoA_Thioesterase.
    MEROPSiS09.A50.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bile acid-CoA:amino acid N-acyltransferase (EC:2.3.1.652 Publications)
    Short name:
    BACAT
    Short name:
    BAT
    Alternative name(s):
    Glycine N-choloyltransferase
    Kan-1
    Long-chain fatty-acyl-CoA hydrolase (EC:3.1.2.2By similarity)
    Gene namesi
    Name:Baat
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 5

    Organism-specific databases

    RGDi2190. Baat.

    Subcellular locationi

    • Peroxisome 1 Publication

    GO - Cellular componenti

    • cytosol Source: Ensembl
    • peroxisome Source: HGNC
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Bile acid-CoA:amino acid N-acyltransferasePRO_0000202161Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401N6-succinyllysineBy similarity
    Modified residuei125 – 1251PhosphoserineCombined sources
    Modified residuei346 – 3461N6-succinyllysineBy similarity
    Modified residuei350 – 3501N6-succinyllysineBy similarity
    Modified residuei409 – 4091N6-succinyllysineBy similarity
    Modified residuei418 – 4181PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ63276.
    PRIDEiQ63276.

    PTM databases

    iPTMnetiQ63276.
    PhosphoSiteiQ63276.

    Expressioni

    Tissue specificityi

    Expressed in liver (at protein level); found in hepatocytes, sinusoidal endothelial cells and Kupffer cells.2 Publications

    Gene expression databases

    GenevisibleiQ63276. RN.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000009777.

    Structurei

    3D structure databases

    ProteinModelPortaliQ63276.
    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.
    InParanoidiQ63276.
    KOiK00659.
    OMAiHSWQEIQ.
    OrthoDBiEOG75TMC9.
    PhylomeDBiQ63276.
    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. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q63276-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKLTAVPLS ALVDEPVHIR VTGLTPFQVV CLQASLKDDK GNLFNSQAFY
    60 70 80 90 100
    RASEVGEVDL ERDSSLGGDY MGVHPMGLFW SMKPEKLLTR LVKRDVMNRP
    110 120 130 140 150
    HKVHIKLCHP YFPVEGKVIS SSLDSLILER WYVAPGVTRI HVKEGRIRGA
    160 170 180 190 200
    LFLPPGEGPF PGVIDLFGGA GGLFEFRASL LASHGFATLA LAYWGYDDLP
    210 220 230 240 250
    SRLEKVDLEY FEEGVEFLLR HPKVLGPGVG ILSVCIGAEI GLSMAINLKQ
    260 270 280 290 300
    ITATVLINGP NFVSSNPHVY RGKVFQPTPC SEEFVTTNAL GLVEFYRTFE
    310 320 330 340 350
    ETADKDSKYC FPIEKAHGHF LFVVGEDDKN LNSKVHAKQA IAQLMKSGKK
    360 370 380 390 400
    NWTLLSYPGA GHLIEPPYSP LCSASRMPFV IPSINWGGEV IPHAAAQEHS
    410 420
    WKEIQKFLKQ HLNPGFNSQL
    Length:420
    Mass (Da):46,465
    Last modified:November 8, 2005 - v2
    Checksum:iAACDB03726EB546F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331V → M in BAA07901 (PubMed:7575455).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D43964 mRNA. Translation: BAA07901.1.
    BC088153 mRNA. Translation: AAH88153.1.
    PIRiS59131.
    RefSeqiNP_058996.2. NM_017300.2.
    UniGeneiRn.11129.

    Genome annotation databases

    EnsembliENSRNOT00000009777; ENSRNOP00000009777; ENSRNOG00000007395.
    GeneIDi29725.
    KEGGirno:29725.
    UCSCiRGD:2190. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D43964 mRNA. Translation: BAA07901.1.
    BC088153 mRNA. Translation: AAH88153.1.
    PIRiS59131.
    RefSeqiNP_058996.2. NM_017300.2.
    UniGeneiRn.11129.

    3D structure databases

    ProteinModelPortaliQ63276.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000009777.

    Protein family/group databases

    ESTHERiratno-BAAT. Acyl-CoA_Thioesterase.
    MEROPSiS09.A50.

    PTM databases

    iPTMnetiQ63276.
    PhosphoSiteiQ63276.

    Proteomic databases

    PaxDbiQ63276.
    PRIDEiQ63276.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000009777; ENSRNOP00000009777; ENSRNOG00000007395.
    GeneIDi29725.
    KEGGirno:29725.
    UCSCiRGD:2190. rat.

    Organism-specific databases

    CTDi570.
    RGDi2190. Baat.

    Phylogenomic databases

    eggNOGiENOG410II3X. Eukaryota.
    COG1073. LUCA.
    GeneTreeiENSGT00390000001046.
    HOGENOMiHOG000116219.
    HOVERGENiHBG000331.
    InParanoidiQ63276.
    KOiK00659.
    OMAiHSWQEIQ.
    OrthoDBiEOG75TMC9.
    PhylomeDBiQ63276.
    TreeFamiTF314911.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14337.
    ReactomeiR-RNO-159418. Recycling of bile acids and salts.
    R-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    SABIO-RKQ63276.

    Miscellaneous databases

    NextBioi610200.
    PROiQ63276.

    Gene expression databases

    GenevisibleiQ63276. RN.

    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. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Reduced expression of kan-1 (encoding putative bile acid-CoA-amino acid N-acyltransferase) mRNA in livers of rats after partial hepatectomy and during sepsis."
      Furutani M., Arii S., Higashitsuji H., Mise M., Fukumoto M., Takano S., Nakayama H., Imamura M., Fujita J.
      Biochem. J. 311:203-208(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: Wistar.
      Tissue: Liver.
    2. "Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization."
      He D., Barnes S., Falany C.N.
      J. Lipid Res. 44:2242-2249(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Liver.
    3. "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].
      Tissue: Liver.
    4. "Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from rat liver."
      Killenberg P.G., Jordan J.T.
      J. Biol. Chem. 253:1005-1010(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
      Tissue: Liver.
    5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
      Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
      Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBAAT_RAT
    AccessioniPrimary (citable) accession number: Q63276
    Secondary accession number(s): Q5M8A2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: May 11, 2016
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Rat BAAT seems to be more efficient at taurine conjugation of cholyl CoA than glycine conjugation. In rat the relative amounts of glycine- and taurine-conjugated bile acids formed in bile are approximately in a ratio of 1:6.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 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.