BAIE_CLOSV
ID BAIE_CLOSV Reviewed; 166 AA.
AC P19412;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Bile acid 7alpha-dehydratase {ECO:0000303|PubMed:8808760};
DE Short=BA7alphaD {ECO:0000303|PubMed:8808760};
DE EC=4.2.1.106 {ECO:0000269|PubMed:8808760};
DE AltName: Full=Bile acid-inducible operon protein E;
DE AltName: Full=C24 bile acid 7alpha-dehydratase {ECO:0000303|PubMed:8808760};
GN Name=baiE {ECO:0000303|PubMed:2254270, ECO:0000303|PubMed:8808760};
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], PROTEIN SEQUENCE OF 1-31, 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, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=JCM 10418 /VPI 12708;
RX PubMed=8808760;
RA Dawson J.A., Mallonee D.H., Bjorkhem I., Hylemon P.B.;
RT "Expression and characterization of a C24 bile acid 7 alpha-dehydratase
RT from Eubacterium sp. strain VPI 12708 in Escherichia coli.";
RL J. Lipid Res. 37:1258-1267(1996).
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 dehydration step in this pathway, yielding a 3-
CC oxo-Delta(4,6)-bile acid-CoA intermediate. In vitro, can act on the
CC free bile acids (non CoA-conjugated) 7-alpha,12-alpha-dihydroxy-3-
CC oxochol-4-enoate and 7-alpha-hydroxy-3-oxochol-4-enoate, but not on 7-
CC alpha,12-alpha-dihydroxy-3-oxo-5-beta-cholanate, 3-alpha,7-alpha,12-
CC alpha-trihydroxy-5-beta-cholanate or 7-beta-hydroxy-3-oxochol-4-enoate.
CC {ECO:0000269|PubMed:8808760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oyl-CoA = 12alpha-
CC hydroxy-3-oxochola-4,6-dien-24-oyl-CoA + H2O; Xref=Rhea:RHEA:10436,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:132977, ChEBI:CHEBI:132978;
CC EC=4.2.1.106; Evidence={ECO:0000305|PubMed:8808760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10437;
CC Evidence={ECO:0000305|PubMed:8808760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha-hydroxy-3-oxochol-4-en-24-oyl-CoA = 3-oxochol-4,6-dien-
CC 24-oyl-CoA + H2O; Xref=Rhea:RHEA:65348, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:140634, ChEBI:CHEBI:140636;
CC Evidence={ECO:0000305|PubMed:8808760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65349;
CC Evidence={ECO:0000305|PubMed:8808760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oate = 12alpha-
CC hydroxy-3-oxochola-4,6-dien-24-oate + H2O; Xref=Rhea:RHEA:65352,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58803, ChEBI:CHEBI:58804;
CC Evidence={ECO:0000269|PubMed:8808760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65353;
CC Evidence={ECO:0000305|PubMed:8808760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha-hydroxy-3-oxochol-4-en-24-oate = 3-oxochola-4,6-dien-
CC 24-oate + H2O; Xref=Rhea:RHEA:47548, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:87747, ChEBI:CHEBI:87748;
CC Evidence={ECO:0000269|PubMed:8808760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47549;
CC Evidence={ECO:0000305|PubMed:8808760};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for 7-alpha,12-alpha-dihydroxy-3-oxochol-4-enoate
CC {ECO:0000269|PubMed:8808760};
CC Vmax=0.48 mmol/min/mg enzyme with 7-alpha,12-alpha-dihydroxy-3-
CC oxochol-4-enoate as substrate {ECO:0000269|PubMed:8808760};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000305|PubMed:8808760}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8808760}.
CC -!- INDUCTION: Induced by bile acids such as cholate.
CC {ECO:0000269|PubMed:2254270}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U57489; AAC45413.1; -; Genomic_DNA.
DR AlphaFoldDB; P19412; -.
DR SMR; P19412; -.
DR SwissLipids; SLP:000001347; -.
DR KEGG; ag:AAC45413; -.
DR BioCyc; MetaCyc:BAIEEUBSP-MON; -.
DR BRENDA; 4.2.1.106; 1513.
DR SABIO-RK; P19412; -.
DR UniPathway; UPA00221; -.
DR GO; GO:0033988; F:bile-acid 7alpha-dehydratase 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 InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR037401; SnoaL-like.
DR Pfam; PF13577; SnoaL_4; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Bile acid catabolism; Direct protein sequencing; Lipid degradation;
KW Lipid metabolism; Lyase; Steroid metabolism.
FT CHAIN 1..166
FT /note="Bile acid 7alpha-dehydratase"
FT /id="PRO_0000064812"
FT CONFLICT 2
FT /note="T -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 19533 MW; 1CBCE86C85ADC3E5 CRC64;
MTLEERVEAL EKELQEMKDI EAIKELKGKY FRCLDGKMWD ELETTLSPNI VTSYSNGKLV
FHSPKEVTDY LKSSMPKEEI SMHMGHTPEI TIDSETTATG RWYLEDRLIF TDGKYKDVGI
NGGAFYTDKY EKIDGQWYIL ETGYVRIYEE HFMRDPKIHI TMNMHK