(data stored in SCRATCH zone)

SWISSPROT: HBD_BACSU

ID   HBD_BACSU               Reviewed;         287 AA.
AC   P45856; O32016;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 138.
DE   RecName: Full=Probable 3-hydroxybutyryl-CoA dehydrogenase;
DE            EC=1.1.1.157;
DE   AltName: Full=Beta-hydroxybutyryl-CoA dehydrogenase;
DE            Short=BHBD;
GN   Name=mmgB; Synonyms=yqiM; OrderedLocusNames=BSU24160;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=8759838; DOI=10.1128/jb.178.16.4778-4786.1996;
RA   Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "A sigma E dependent operon subject to catabolite repression during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 178:4778-4786(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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   [4]
RP   SEQUENCE REVISION.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) +
CC         NADPH; Xref=Rhea:RHEA:16197, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286,
CC         ChEBI:CHEBI:57316, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.157;
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the mother cell at intermediate
CC       stages of sporulation under the control of the sigma-E factor.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- INDUCTION: Subject to catabolite repression.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; U29084; AAB09614.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12588.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB14347.2; -; Genomic_DNA.
DR   PIR; C69658; C69658.
DR   RefSeq; NP_390296.2; NC_000964.3.
DR   RefSeq; WP_003230294.1; NZ_JNCM01000036.1.
DR   SMR; P45856; -.
DR   STRING; 224308.BSU24160; -.
DR   PaxDb; P45856; -.
DR   PRIDE; P45856; -.
DR   EnsemblBacteria; CAB14347; CAB14347; BSU24160.
DR   GeneID; 938660; -.
DR   KEGG; bsu:BSU24160; -.
DR   PATRIC; fig|224308.179.peg.2630; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000141498; -.
DR   InParanoid; P45856; -.
DR   KO; K00074; -.
DR   OMA; MAHPMGP; -.
DR   PhylomeDB; P45856; -.
DR   BioCyc; BSUB:BSU24160-MONOMER; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
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; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P45856.
DR   SWISS-2DPAGE; P45856.
KW   Fatty acid metabolism; Lipid metabolism; NADP; Oxidoreductase;
KW   Reference proteome; Sporulation.
FT   CHAIN           1..287
FT                   /note="Probable 3-hydroxybutyryl-CoA dehydrogenase"
FT                   /id="PRO_0000109255"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        209..211
FT                   /note="AKP -> RT (in Ref. 2; BAA12588)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  31394 MW;  60BF1DBBEDEBA05F CRC64;
     MEIKQIMVAG AGQMGSGIAQ TAADAGFYVR MYDVNPEAAE AGLKRLKKQL ARDAEKGKRT
     ETEVKSVINR ISISQTLEEA EHADIVIEAI AENMAAKTEM FKTLDRICPP HTILASNTSS
     LPITEIAAVT NRPQRVIGMH FMNPVPVMKL VEVIRGLATS EETALDVMAL AEKMGKTAVE
     VNDFPGFVSN RVLLPMINEA IYCVYEGVAK PEAIDEVMKL GMNHPMGPLA LADFIGLDTC
     LSIMEVLHSG LGDSKYRPCP LLRKYVKAGW LGKKSGRGFY DYEEKTS
//

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