BAICD_CLOSV
ID BAICD_CLOSV Reviewed; 639 AA.
AC P19410; P19411;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=3-oxocholoyl-CoA 4-desaturase {ECO:0000305};
DE EC=1.3.1.115 {ECO:0000269|PubMed:18047844};
DE AltName: Full=Bile acid-inducible operon protein C;
DE AltName: Full=Bile acid-inducible operon protein CD;
DE AltName: Full=Bile acid-inducible operon protein D;
GN Name=baiCD {ECO:0000303|PubMed:18047844};
GN Synonyms=baiC {ECO:0000303|PubMed:2254270},
GN baiD {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].
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 SEQUENCE REVISION.
RA Kang D.-J., Ridlon J.M., Moore D.R. II, Barnes S., Hylemon P.B.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=18047844; DOI=10.1016/j.bbalip.2007.10.008;
RA Kang D.J., Ridlon J.M., Moore D.R. II, Barnes S., Hylemon P.B.;
RT "Clostridium scindens baiCD and baiH genes encode stereo-specific
RT 7alpha/7beta-hydroxy-3-oxo-delta4-cholenoic acid oxidoreductases.";
RL Biochim. Biophys. Acta 1781:16-25(2008).
CC -!- FUNCTION: Stereo-specific NAD(H)-dependent 3-oxo-delta4-cholenoic acid
CC oxidoreductase involved in bile acid 7alpha-dehydroxylation.
CC {ECO:0000269|PubMed:18047844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha,12alpha-dihydroxy-3-oxochol-24-oyl-CoA + NAD(+) =
CC 7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:56664, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132977, ChEBI:CHEBI:136700;
CC EC=1.3.1.115; Evidence={ECO:0000269|PubMed:18047844};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7alpha-hydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7alpha-hydroxy-
CC 3-oxochol-4-en-24-oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:56660,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:136698, ChEBI:CHEBI:140636; EC=1.3.1.115;
CC Evidence={ECO:0000269|PubMed:18047844};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- PATHWAY: Lipid metabolism; bile acid degradation.
CC {ECO:0000305|PubMed:18047844}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the product of two separate ORFs,
CC baiC and baiD. {ECO:0000305|PubMed:2254270}.
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DR EMBL; U57489; AAC45411.2; -; Genomic_DNA.
DR RefSeq; WP_025645824.1; NZ_CP080442.1.
DR AlphaFoldDB; P19410; -.
DR SMR; P19410; -.
DR PRIDE; P19410; -.
DR KEGG; ag:AAC45411; -.
DR BioCyc; MetaCyc:BAI3OXOEUBSP-MON; -.
DR BRENDA; 1.3.1.115; 1513.
DR UniPathway; UPA00279; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Bile acid catabolism; FAD; Flavoprotein; FMN; Iron; Iron-sulfur;
KW Lipid degradation; Lipid metabolism; Metal-binding; NAD; Oxidoreductase;
KW Steroid metabolism.
FT CHAIN 1..639
FT /note="3-oxocholoyl-CoA 4-desaturase"
FT /id="PRO_0000194469"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 286
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 308..309
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 332
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 335
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 339
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 353
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 420
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 447
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
SQ SEQUENCE 639 AA; 70274 MW; 28CD484858CF2123 CRC64;
MSYEALFSPF KVRGLELKNR IVLPGMNTKM AKNKHDIGED MIAYHVARAK AGCALNIFEC
VALCPAPHAY MYMGLYTDHH VEQLKKLTDA VHEAGGKMGI QLWHGGFSPQ MFFDETNTLE
TPDTLTVERI HEIVEEFGRG ARMAVQAGFD AVEFHAAHSY LPHEFLSPGM NKRTDEYGGS
FENRCRFCYE VVQAIRSNIP DDMPFFMRAD CIDELMEQTM TEEEIVTFIN KCAELGVDVA
DLSRGNATSF ATVYEVPPFN LAHGFNIENI YNIKKQINIP VMGVGRINTG EMANKVIEEG
KFDLVGIGRA QLADPNWITK VREGKEDLIR HCIGCDQGCY DAVINPKMKH ITCTHNPGLC
LEYQGMPKTD APKKVMIVGG GMAGMIAAEV LKTRGHNPVI FEASDKLAGQ FRLAGVAPMK
QDWADVAEWE AKEVERLGIE VRLNTEVTAE TIKEFNPDNV IIAVGSTYAL PEIPGIDSPS
VYSQYQVLKG EVNPTGRVAV IGCGLVGTEV AELLASRGAQ VIAIERKGVG TGLSMLRRMF
MNPEFKYYKI AKMSGTNVTA LEQGKVHYIM TDKKTKEVTQ GVLECDATVI CTGITARPSD
GLKARCEELG IPVEVIGDAA GARDCTIATR EGYDAGMAI
