BAIB_CLOSV
ID BAIB_CLOSV Reviewed; 520 AA.
AC P19409;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Bile acid--coenzyme A ligase {ECO:0000303|PubMed:1551828};
DE EC=6.2.1.7 {ECO:0000269|PubMed:1551828};
DE AltName: Full=Cholate--CoA ligase {ECO:0000305};
GN Name=baiB {ECO:0000303|PubMed:1551828, ECO:0000303|PubMed:2254270};
OS Clostridium scindens (strain JCM 10418 / VPI 12708).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=29347;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=2254270; DOI=10.1128/jb.172.12.7011-7019.1990;
RA Mallonee D.H., White W.B., Hylemon P.B.;
RT "Cloning and sequencing of a bile acid-inducible operon from Eubacterium
RT sp. strain VPI 12708.";
RL J. Bacteriol. 172:7011-7019(1990).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=1551828; DOI=10.1128/jb.174.7.2065-2071.1992;
RA Mallonee D.H., Adams J.L., Hylemon P.B.;
RT "The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708
RT encodes a bile acid-coenzyme A ligase.";
RL J. Bacteriol. 174:2065-2071(1992).
CC -!- FUNCTION: Functions in the bile acid 7alpha-dehydroxylation pathway,
CC which forms secondary bile acids via the 7alpha-dehydroxylation of
CC primary bile acids, and is carried out by intestinal anaerobic
CC bacteria. Catalyzes the initial step in this pathway, i.e. the ATP-
CC dependent thioesterification of primary bile acids with coenzyme A. Is
CC active with C-24 bile acids with free carboxyl groups such as cholate,
CC deoxycholate and chenodeoxycholate. Produces AMP and pyrophosphate in
CC addition to the bile acid-CoA thioester. {ECO:0000269|PubMed:1551828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:23532, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:456215; EC=6.2.1.7;
CC Evidence={ECO:0000269|PubMed:1551828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533;
CC Evidence={ECO:0000305|PubMed:1551828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + deoxycholate = AMP + deoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:47128, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58810, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:1551828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47129;
CC Evidence={ECO:0000305|PubMed:1551828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:43764, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62989, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:1551828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765;
CC Evidence={ECO:0000305|PubMed:1551828};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1551828};
CC -!- ACTIVITY REGULATION: Inhibited by diphosphate.
CC {ECO:0000269|PubMed:1551828}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for cholate {ECO:0000269|PubMed:1551828};
CC KM=200 uM for ATP {ECO:0000269|PubMed:1551828};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:1551828};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000305|PubMed:1551828}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:1551828}.
CC -!- INDUCTION: Induced by bile acids such as cholate.
CC {ECO:0000269|PubMed:2254270}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; U57489; AAC45410.1; -; Genomic_DNA.
DR PDB; 4LGC; X-ray; 2.19 A; A=1-520.
DR PDBsum; 4LGC; -.
DR AlphaFoldDB; P19409; -.
DR SMR; P19409; -.
DR SwissLipids; SLP:000001349; -.
DR KEGG; ag:AAC45410; -.
DR BioCyc; MetaCyc:BAIBEUBSP-MON; -.
DR UniPathway; UPA00221; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047747; F:cholate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Bile acid catabolism; Ligase; Lipid degradation;
KW Lipid metabolism; Nucleotide-binding; Steroid metabolism.
FT CHAIN 1..520
FT /note="Bile acid--coenzyme A ligase"
FT /id="PRO_0000193063"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:4LGC"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4LGC"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:4LGC"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:4LGC"
SQ SEQUENCE 520 AA; 58294 MW; 871254FDF6852CC4 CRC64;
MHKKSACERE GKELKRDFFN KFNLGTSNFV TPGKQLEYVS ECKPDSTAVI CLDKEQNCSV
ITWHQLHVYS SQLAWYLIEN EIGPGSIVLT MFPNSIEHII AVFAIWKAGA CYMPMSYKAA
ESEIREACDT IHPNAAFAEC KIPGLKFCLS ADEIYEAMEG RSKEMPSDRL ANPNMISLSG
GTSGKMKFIR QNLPCGLDDE TIRSWSLMSG MGFEQRQLLV GPLFHGAPHS AAFNGLFMGN
TLVLTRNLCP GNILNMIKKY KIEFIQMVPT LMNRLAKLEG VGKEDFASLK ALCHTGGVCS
PWLKQIWIDL LGPEKIYEMY SMTECIGLTC IRGDEWVKHP GSIGRPVGDS KVSIRDENGK
EVAPFEIGEI YMTAPASYLV TEYINWEPLE VKEGGFRSVG DIGYVDEQGY LYFSDRRSDM
LVSGGENVFA TEVETALLRY KDILDAVVVG IPDEDLGRRL HAVIETGKEI PAEELKTFLR
KYLTPYKIPK TFEFVRSIRR GDNGKADRKR ILEDCIARGG
