BAIH_CLOSV
ID BAIH_CLOSV Reviewed; 661 AA.
AC P32370;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=7-beta-hydroxy-3-oxochol-24-oyl-CoA 4-desaturase {ECO:0000305};
DE EC=1.3.1.116 {ECO:0000269|PubMed:18047844};
DE AltName: Full=NADH-dependent flavin oxidoreductase {ECO:0000303|PubMed:8491719};
DE AltName: Full=NADH:flavin oxidoreductase {ECO:0000303|PubMed:8491719};
DE Short=NADH:FOR {ECO:0000303|PubMed:8491719};
GN Name=baiH {ECO:0000303|PubMed:8491719};
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 1-25, FUNCTION AS A
RP FLAVIN OXIDOREDUCTASE, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP INDUCTION.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=8491719; DOI=10.1128/jb.175.10.3002-3012.1993;
RA Franklund C.V., Baron S.F., Hylemon P.B.;
RT "Characterization of the baiH gene encoding a bile acid-inducible
RT NADH:flavin oxidoreductase from Eubacterium sp. strain VPI 12708.";
RL J. Bacteriol. 175:3002-3012(1993).
RN [2]
RP FUNCTION AS A FLAVIN OXIDOREDUCTASE, COFACTOR, AND SUBUNIT.
RC STRAIN=JCM 10418 / VPI 12708;
RX PubMed=7599167; DOI=10.1016/0167-4838(95)00034-r;
RA Baron S.F., Hylemon P.B.;
RT "Expression of the bile acid-inducible NADH:flavin oxidoreductase gene of
RT Eubacterium sp. VPI 12708 in Escherichia coli.";
RL Biochim. Biophys. Acta 1249:145-154(1995).
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: NADH-dependent flavin oxidoreductase (PubMed:8491719,
CC PubMed:7599167, PubMed:18047844). Stereo-specific NAD(H)-dependent 3-
CC oxo-delta4-cholenoic acid oxidoreductase involved in bile acid 7beta-
CC dehydroxylation (PubMed:18047844). {ECO:0000269|PubMed:18047844,
CC ECO:0000269|PubMed:7599167, ECO:0000269|PubMed:8491719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7beta-hydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7beta-hydroxy-3-
CC oxochol-4-en-24-oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:56668,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:140637, ChEBI:CHEBI:140638; EC=1.3.1.116;
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:0000269|PubMed:7599167, ECO:0000269|PubMed:8491719};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- ACTIVITY REGULATION: Activity is inhibited by sulfhydryl-reactive
CC compounds, acriflavine, o-phenanthroline and EDTA.
CC {ECO:0000269|PubMed:8491719}.
CC -!- PATHWAY: Lipid metabolism; bile acid degradation.
CC {ECO:0000305|PubMed:18047844}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:7599167,
CC ECO:0000269|PubMed:8491719}.
CC -!- INDUCTION: Induced by cholate. {ECO:0000269|PubMed:8491719}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000305}.
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DR EMBL; U57489; AAC45417.1; -; Genomic_DNA.
DR AlphaFoldDB; P32370; -.
DR SMR; P32370; -.
DR PRIDE; P32370; -.
DR KEGG; ag:AAC45417; -.
DR BioCyc; MetaCyc:MON-19700; -.
DR BRENDA; 1.3.1.116; 1513.
DR BRENDA; 1.5.1.36; 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; Direct protein sequencing; FAD; Flavoprotein;
KW FMN; Iron; Iron-sulfur; Lipid degradation; Lipid metabolism; Metal-binding;
KW NAD; Oxidoreductase; Steroid metabolism.
FT CHAIN 1..661
FT /note="7-beta-hydroxy-3-oxochol-24-oyl-CoA 4-desaturase"
FT /id="PRO_0000194470"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 168..171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 298
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 320..321
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 344
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 351
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 363
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 394
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 421
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT CONFLICT 22
FT /note="R -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 72029 MW; EC81F28A3714BAC9 CRC64;
MDMKHSRLFS PLQIGSLTLS NRVGMAPMSM DYEAADGTVP KRLADVFVRR AEGGTGYVMI
DAVTIDSKYP YMGNTTALDR DELVPQFKEF ADRVKEAGST LVPQIIHPGP ESVCGYRHIA
PLGPSANTNA NCHVSRSISI DEIHDIIKQF GQAARRAEEA GCGAISLHCA HAYMLPGSFL
SPLRNKRMDE YGGSLDNRAR FVIEMIEEAR RNVSPDFPIF LRISGDERMV GGNSLEDMLY
LAPKFEAAGV SMLEVSGGTQ YEGLEHIIPC QNKSRGVNVY EASEIKKVVG IPVYAVGKIN
DIRYAAEIVE RGLVDGVAMG RPLLADPDLC KKAVEGQFDE ITPCASCGGS CISRSEAAPE
CHCHINPRLG REYEFPDVPA EKSKKVLVIG AGPGGMMAAV TAAERGHDVT VWEADDKIGG
QLNLAVVAPG KQEMTQWMVH LNYRAKKAGV KFEFNKEATA EDVKALAPEA VIVATGAKPL
VPPIKGTQDY PVLTAHDFLR GKFVIPKGRV CVLGGGAVAC ETAETALENA RPNSYTRGYD
ASIGDIDVTL VEMLPQLLTG VCAPNREPLI RKLKSKGVHI NVNTKIMEVT DHEVKVQRQD
GTQEWLEGFD YVLFGLGSRN YDPLSETLKE FVPEVHVIGD AVRARQASYA MWEGFEKAYS
L
