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Protein

Bile acid-CoA:amino acid N-acyltransferase

Gene

Baat

Organism
Mus musculus (Mouse)
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 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.1 Publication
Palmitoyl-CoA + H2O = CoA + palmitate.By similarity

Kineticsi

  1. KM=1.9 mM for taurine1 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

    ReactomeiR-MMU-159418. Recycling of bile acids and salts.
    R-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    SABIO-RKQ91X34.

    Protein family/group databases

    ESTHERimouse-BAAT. Acyl-CoA_Thioesterase.
    MEROPSiS09.A50.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bile acid-CoA:amino acid N-acyltransferase (EC:2.3.1.651 Publication)
    Short name:
    BACAT
    Short name:
    BAT
    Alternative name(s):
    Glycine N-choloyltransferase
    Long-chain fatty-acyl-CoA hydrolase (EC:3.1.2.2By similarity)
    Gene namesi
    Name:Baat
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 4

    Organism-specific databases

    MGIiMGI:106642. Baat.

    Subcellular locationi

    • Cytoplasm By similarity
    • Peroxisome By similarity

    • Note: Cytoplasmic or/and peroxisomal.By similarity

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • peroxisome Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Bile acid-CoA:amino acid N-acyltransferasePRO_0000202160Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiQ91X34.
    MaxQBiQ91X34.
    PaxDbiQ91X34.
    PRIDEiQ91X34.

    PTM databases

    iPTMnetiQ91X34.
    PhosphoSiteiQ91X34.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, kidney, gallbladder, proximal intestine and distal intestine. Weakly expressed in adrenal gland, lung, brain and muscle.2 Publications

    Gene expression databases

    BgeeiQ91X34.
    GenevisibleiQ91X34. MM.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    GO - Molecular functioni

    Protein-protein interaction databases

    IntActiQ91X34. 3 interactions.
    MINTiMINT-1854394.
    STRINGi10090.ENSMUSP00000041983.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91X34.
    SMRiQ91X34. Positions 14-412.
    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.
    InParanoidiQ91X34.
    KOiK00659.
    OMAiPERIGMV.
    OrthoDBiEOG75TMC9.
    PhylomeDBiQ91X34.
    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.

    Q91X34-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKLTAVPLS ALVDEPVHIQ VTGLAPFQVV CLQASLKDEK GNLFSSQAFY
    60 70 80 90 100
    RASEVGEVDL EHDPSLGGDY MGVHPMGLFW SLKPEKLLGR LIKRDVMNSP
    110 120 130 140 150
    YQIHIKACHP YFPLQDIVVS PPLDSLTLER WYVAPGVKRI QVKESRIRGA
    160 170 180 190 200
    LFLPPGEGPF PGVIDLFGGA GGLMEFRASL LASRGFATLA LAYWNYDDLP
    210 220 230 240 250
    SRLEKVDLEY FEEGVEFLLR HPKVLGPGVG ILSVCIGAEI GLSMAINLKQ
    260 270 280 290 300
    IRATVLINGP NFVSQSPHVY HGQVYPPVPS NEEFVVTNAL GLVEFYRTFQ
    310 320 330 340 350
    ETADKDSKYC FPIEKAHGHF LFVVGEDDKN LNSKVHANQA IAQLMKNGKK
    360 370 380 390 400
    NWTLLSYPGA GHLIEPPYTP LCQASRMPIL IPSLSWGGEV IPHAAAQEHS
    410 420
    WKEIQKFLKQ HLLPDLSSQL
    Length:420
    Mass (Da):46,482
    Last modified:December 1, 2001 - v1
    Checksum:iAABC6DB573C5EF50
    GO

    Sequence cautioni

    The sequence AAB58325.1 differs from that shown. Reason: Frameshift at positions 40 and 44. Curated
    The sequence BAC25534.1 differs from that shown. Reason: Frameshift at position 63. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971M → I in AAB58325 (PubMed:9215542).Curated
    Sequence conflicti117 – 1171I → L in AAB58325 (PubMed:9215542).Curated
    Sequence conflicti268 – 2681H → Q in BAC25534 (PubMed:16141072).Curated
    Sequence conflicti385 – 3851S → R in BAC25534 (PubMed:16141072).Curated
    Sequence conflicti394 – 3941A → SQ in AAB58325 (PubMed:9215542).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U95215 mRNA. Translation: AAB58325.1. Frameshift.
    AK017923 mRNA. Translation: BAC25534.1. Frameshift.
    AL772310 Genomic DNA. Translation: CAM21769.1.
    CH466565 Genomic DNA. Translation: EDL02319.1.
    BC012683 mRNA. No translation available.
    CCDSiCCDS18173.1.
    RefSeqiNP_031545.2. NM_007519.3.
    UniGeneiMm.2859.

    Genome annotation databases

    EnsembliENSMUST00000043056; ENSMUSP00000041983; ENSMUSG00000039653.
    ENSMUST00000166036; ENSMUSP00000129603; ENSMUSG00000039653.
    GeneIDi12012.
    KEGGimmu:12012.
    UCSCiuc008svt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U95215 mRNA. Translation: AAB58325.1. Frameshift.
    AK017923 mRNA. Translation: BAC25534.1. Frameshift.
    AL772310 Genomic DNA. Translation: CAM21769.1.
    CH466565 Genomic DNA. Translation: EDL02319.1.
    BC012683 mRNA. No translation available.
    CCDSiCCDS18173.1.
    RefSeqiNP_031545.2. NM_007519.3.
    UniGeneiMm.2859.

    3D structure databases

    ProteinModelPortaliQ91X34.
    SMRiQ91X34. Positions 14-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ91X34. 3 interactions.
    MINTiMINT-1854394.
    STRINGi10090.ENSMUSP00000041983.

    Protein family/group databases

    ESTHERimouse-BAAT. Acyl-CoA_Thioesterase.
    MEROPSiS09.A50.

    PTM databases

    iPTMnetiQ91X34.
    PhosphoSiteiQ91X34.

    Proteomic databases

    EPDiQ91X34.
    MaxQBiQ91X34.
    PaxDbiQ91X34.
    PRIDEiQ91X34.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000043056; ENSMUSP00000041983; ENSMUSG00000039653.
    ENSMUST00000166036; ENSMUSP00000129603; ENSMUSG00000039653.
    GeneIDi12012.
    KEGGimmu:12012.
    UCSCiuc008svt.2. mouse.

    Organism-specific databases

    CTDi570.
    MGIiMGI:106642. Baat.

    Phylogenomic databases

    eggNOGiENOG410II3X. Eukaryota.
    COG1073. LUCA.
    GeneTreeiENSGT00390000001046.
    HOGENOMiHOG000116219.
    HOVERGENiHBG000331.
    InParanoidiQ91X34.
    KOiK00659.
    OMAiPERIGMV.
    OrthoDBiEOG75TMC9.
    PhylomeDBiQ91X34.
    TreeFamiTF314911.

    Enzyme and pathway databases

    ReactomeiR-MMU-159418. Recycling of bile acids and salts.
    R-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    SABIO-RKQ91X34.

    Miscellaneous databases

    PROiQ91X34.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ91X34.
    GenevisibleiQ91X34. MM.

    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. "Cloning, expression, and chromosomal localization of mouse liver bile acid CoA:amino acid N-acyltransferase."
      Falany C.N., Fortinberry H., Leiter E.H., Barnes S.
      J. Lipid Res. 38:1139-1148(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Strain: FVB/N.
      Tissue: Liver.
    6. "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: TISSUE SPECIFICITY.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-346; LYS-350 AND LYS-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiBAAT_MOUSE
    AccessioniPrimary (citable) accession number: Q91X34
    Secondary accession number(s): A2AKK7, O08833, Q8C1I3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: December 1, 2001
    Last modified: June 8, 2016
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mouse BAAT seems to be selective for taurine conjugation of cholyl CoA. In mouse only taurine-conjugated bile acids are found in bile.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. 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.