FADH_BACSU
ID FADH_BACSU Reviewed; 254 AA.
AC O34717;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing];
DE EC=1.3.1.34 {ECO:0000305};
GN Name=fadH; Synonyms=ykuF; OrderedLocusNames=BSU14060;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Scanlan E., Devine K.M.;
RT "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP GENE NAME, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17189250; DOI=10.1074/jbc.m606831200;
RA Matsuoka H., Hirooka K., Fujita Y.;
RT "Organization and function of the YsiA regulon of Bacillus subtilis
RT involved in fatty acid degradation.";
RL J. Biol. Chem. 282:5180-5194(2007).
CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the
CC metabolism of unsaturated fatty enoyl-CoA esters having double bonds in
CC both even- and odd-numbered positions. Catalyzes the NADP-dependent
CC reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4,5-saturated-(2E)-enoyl-CoA + NADP(+) = a (2E,4E)-dienoyl-
CC CoA + H(+) + NADPH; Xref=Rhea:RHEA:12136, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85100,
CC ChEBI:CHEBI:85101; EC=1.3.1.34;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(2E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45232, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099,
CC ChEBI:CHEBI:85100; EC=1.3.1.34;
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of
CC 14-20 carbon atoms). When LCFAs are present in the medium, they are
CC converted to long-chain acyl-CoAs, which antagonize FadR as to its
CC binding to fadR boxes on target DNA and thus derepress transcription.
CC {ECO:0000269|PubMed:17189250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}.
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DR EMBL; AJ222587; CAA10869.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13279.1; -; Genomic_DNA.
DR PIR; C69865; C69865.
DR RefSeq; NP_389289.1; NC_000964.3.
DR RefSeq; WP_003232398.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34717; -.
DR SMR; O34717; -.
DR STRING; 224308.BSU14060; -.
DR PaxDb; O34717; -.
DR EnsemblBacteria; CAB13279; CAB13279; BSU_14060.
DR GeneID; 939226; -.
DR KEGG; bsu:BSU14060; -.
DR PATRIC; fig|224308.179.peg.1533; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; O34717; -.
DR OMA; GSICSAQ; -.
DR PhylomeDB; O34717; -.
DR BioCyc; BSUB:BSU14060-MON; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR InterPro; IPR045017; DECR2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43296; PTHR43296; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Fatty acid metabolism; Lipid degradation; Lipid metabolism; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..254
FT /note="Probable 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-
FT producing]"
FT /id="PRO_0000054846"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 6..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 254 AA; 27126 MW; EDD9D1DD2B1707BF CRC64;
MEKKAVIITG GSSGMGKAMA KKQAELGWHV MVTGRNHEAL EETKKEIQTF EGQVACFQMD
VRSDSAASDM IKEAVKAFGR LDALINNAAG NFICPAEKLT PNGWKAVIEI VLNGTFFCSQ
AAARHWIDQK QQGVILNMAA TYAWGAGAGV VHSAAAKAGV LSLTRTLAVE WGSKYGIRTN
AIAPGPIERT GGAEKLFESE KAMARTMNSV PLGRLGTPEE IAALAAFLLS DEASYINGDC
ITMDGGQWLN PYPF
