ID   FADB_BACSU              Reviewed;         258 AA.
AC   P94549; Q795X7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 128.
DE   RecName: Full=Probable enoyl-CoA hydratase;
DE            EC=4.2.1.17;
GN   Name=fadB; Synonyms=ysiB; OrderedLocusNames=BSU28540;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
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: Involved in the degradation of long-chain fatty acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
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 enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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; Z75208; CAA99573.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14814.1; -; Genomic_DNA.
DR   PIR; G69985; G69985.
DR   RefSeq; NP_390732.1; NC_000964.3.
DR   RefSeq; WP_003229549.1; NC_000964.3.
DR   AlphaFoldDB; P94549; -.
DR   SMR; P94549; -.
DR   FunCoup; P94549; 62.
DR   STRING; 224308.BSU28540; -.
DR   jPOST; P94549; -.
DR   PaxDb; 224308-BSU28540; -.
DR   EnsemblBacteria; CAB14814; CAB14814; BSU_28540.
DR   GeneID; 937448; -.
DR   KEGG; bsu:BSU28540; -.
DR   PATRIC; fig|224308.179.peg.3101; -.
DR   eggNOG; COG1024; Bacteria.
DR   InParanoid; P94549; -.
DR   OrthoDB; 9775794at2; -.
DR   PhylomeDB; P94549; -.
DR   BioCyc; BSUB:BSU28540-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P94549; -.
DR   GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IEA:RHEA.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   CDD; cd06558; crotonase-like; 1.
DR   FunFam; 3.90.226.10:FF:000009; Carnitinyl-CoA dehydratase; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   NCBIfam; NF005803; PRK07658.1; 1.
DR   PANTHER; PTHR11941; ENOYL-COA HYDRATASE-RELATED; 1.
DR   PANTHER; PTHR11941:SF175; ENOYL-COA HYDRATASE-RELATED; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid metabolism; Lipid degradation; Lipid metabolism; Lyase;
KW   Reference proteome.
FT   CHAIN           1..258
FT                   /note="Probable enoyl-CoA hydratase"
FT                   /id="PRO_0000360671"
SQ   SEQUENCE   258 AA;  27554 MW;  5C1B3C3119C6F860 CRC64;
     MNAISLAVDQ FVAVLTIHNP PANALSSRIL EELSSCLDQC ETDAGVRSII IHGEGRFFSA
     GADIKEFTSL KGNEDSSLLA ERGQQLMERI ESFPKPIIAA IHGAALGGGL ELAMACHIRI
     AAEDAKLGLP ELNLGIIPGF AGTQRLPRYV GTAKALELIG SGEPISGKEA LDLGLVSIGA
     KDEAEVIEKA KALAAKFAEK SPQTLASLLE LLYSNKVYSY EGSLKLEAKR FGEAFESEDA
     KEGIQAFLEK RKPQFKGE
//