ID   FADN_BACSU              Reviewed;         789 AA.
AC   O32178;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable 3-hydroxyacyl-CoA dehydrogenase;
DE            EC=1.1.1.35;
GN   Name=fadN; Synonyms=yusL; OrderedLocusNames=BSU32840;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   INDUCTION, GENE NAME, AND IDENTIFICATION OF INITIATION SITE.
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 + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
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 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB15273.2; -; Genomic_DNA.
DR   PIR; E70021; E70021.
DR   RefSeq; NP_391163.1; NC_000964.3.
DR   RefSeq; WP_003243831.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32178; -.
DR   SMR; O32178; -.
DR   STRING; 224308.BSU32840; -.
DR   jPOST; O32178; -.
DR   PaxDb; O32178; -.
DR   PRIDE; O32178; -.
DR   EnsemblBacteria; CAB15273; CAB15273; BSU_32840.
DR   GeneID; 937125; -.
DR   KEGG; bsu:BSU32840; -.
DR   PATRIC; fig|224308.179.peg.3558; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   InParanoid; O32178; -.
DR   OMA; GQGFYKK; -.
DR   BioCyc; BSUB:BSU32840-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid metabolism; Lipid degradation; Lipid metabolism; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..789
FT                   /note="Probable 3-hydroxyacyl-CoA dehydrogenase"
FT                   /id="PRO_0000360673"
SQ   SEQUENCE   789 AA;  87085 MW;  9379318D7E70F40C CRC64;
     MHKHIRKAAV LGSGVMGSGI AAHLANIGIP VLLLDIVPND LTKEEEKKGL TKDSSEVRSR
     LSRQAMKKLL KQKPAPLTSA KNTSYITPGN LEDDAEKLKE ADWIIEVVVE NLEVKKKIFA
     LVDEHRKTGS IVSSNTSGIS VQEMAEGRSD DFKAHFLGTH FFNPARYLKL LEIIPIKETD
     PDILKFMTAF GENVLGKGVV TAKDTPNFIA NRIGTYGLLV TVQEMLKGGY QVGEVDSITG
     PLIGRPKSAT FRTLDVVGLD TFAHVARNVY DKADGDEKEV FRIPSFMNDM LEKGWIGSKA
     GQGFYKKEGK TIYELDPVTL TYGERTKMKS PALEAAKQAK GTKAKMKALI YSDDRAGRLL
     WNITSQTLLY SAELLGEIAD DIHAIDQAMK WGFGWELGPF EMWDAIGLKQ SAEKLEQLGA
     DMPGWIKEML DKGNETFYIK ENGTVFYYDR GEYRAVKENK KRIHLQALKE TKGVIAKNSG
     ASLIDLGDDV ALLEFHSKSN AIGLDIIQMI HKGLEETERN YKGLVIGNQG KNFCVGANLA
     MILMEVQDDN FLEVDFVIRR FQETMMKIKY SAKPVVAAPF GMTLGGGTEA CLPAARIQAA
     SEAYMGLVES GVGLIPGGGG NKELYINHLR RGHDPMNAAM KTFETIAMAK VSASAQEARE
     MNILKETDQI SVNQDHLLYD AKQLAASLYD TGWRPPVKEK VKVPGETGYA ALLLGAEQMK
     LSGYISEHDF KIAKKLAYVI AGGKVPFGTE VDEEYLLEIE REAFLSLSGE AKSQARMQHM
     LVKGKPLRN