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Database: UniProt
Entry: HBD_SYNWW
LinkDB: HBD_SYNWW
Original site: HBD_SYNWW 
ID   HBD_SYNWW               Reviewed;         279 AA.
AC   Q0AVM2;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000303|PubMed:23468890};
DE            EC=1.1.1.35 {ECO:0000305|PubMed:23468890};
GN   OrderedLocusNames=Swol_1935 {ECO:0000312|EMBL:ABI69232.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP   FUNCTION, AND PATHWAY.
RX   PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA   Schmidt A., Mueller N., Schink B., Schleheck D.;
RT   "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT   Syntrophomonas wolfei.";
RL   PLoS ONE 8:E56905-E56905(2013).
CC   -!- FUNCTION: Involved in syntrophic growth of S.wolfei with butyrate, as
CC       part of the butyrate oxidation pathway. Probably catalyzes the
CC       oxidation of 3-hydroxybutyryl-CoA to acetoacetyl-CoA.
CC       {ECO:0000305|PubMed:23468890}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:42048, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78611;
CC         Evidence={ECO:0000305|PubMed:23468890};
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         Evidence={ECO:0000305|PubMed:23468890};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000305|PubMed:23468890}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}.
CC   -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC       protein level). Seems to be constitutively expressed.
CC       {ECO:0000269|PubMed:23468890}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000448; ABI69232.1; -; Genomic_DNA.
DR   RefSeq; WP_011641325.1; NC_008346.1.
DR   AlphaFoldDB; Q0AVM2; -.
DR   SMR; Q0AVM2; -.
DR   STRING; 335541.Swol_1935; -.
DR   KEGG; swo:Swol_1935; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_2_0_9; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003857; F:3-hydroxyacyl-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:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Fatty acid metabolism; Lipid metabolism; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..279
FT                   /note="3-hydroxybutyryl-CoA dehydrogenase"
FT                   /id="PRO_0000442214"
SQ   SEQUENCE   279 AA;  29762 MW;  78205CA5EA5B92B0 CRC64;
     MKIMVLGAGT MGAGIVQTAA QAGFEVVVRD IKQEFVDRGI AGIDKLLSKN VDKGRMTAED
     KAAVMGRISG TVDMGAAADC DLVIEAALEV MDIKKAIFKE LDSICKPECI LASNTSALSV
     TEIAAATGRA DKVIGMHFFN PVPAMKLVEV IRGASTSQAT YDAIKDLSVK MGKSPVEINE
     APGFVVNRLL IPMLNEGMYC LMEGVANAAD IDTSMKFGAG HPMGPLALAD MIGLDICLKI
     METLYKEFGD PKYRPCPLLA KMVRANKLGR KTGEGFFAY
//
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