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Database: UniProt
Entry: A6LQ83_CLOB8
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ID   A6LQ83_CLOB8            Unreviewed;       282 AA.
AC   A6LQ83;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:ABR32513.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:ABR32513.1};
GN   OrderedLocusNames=Cbei_0325 {ECO:0000313|EMBL:ABR32513.1};
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR32513.1, ECO:0000313|Proteomes:UP000000565};
RN   [1] {ECO:0000313|EMBL:ABR32513.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR32513.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=21962126; DOI=10.1186/1471-2164-12-479;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Single-nucleotide resolution analysis of the transcriptome structure of
RT   Clostridium beijerinckii NCIMB 8052 using RNA-Seq.";
RL   BMC Genomics 12:479-479(2011).
RN   [3] {ECO:0000313|EMBL:ABR32513.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=22433311; DOI=10.1186/1471-2164-13-102;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Genome-wide dynamic transcriptional profiling in clostridium beijerinckii
RT   NCIMB 8052 using single-nucleotide resolution RNA-Seq.";
RL   BMC Genomics 13:102-102(2012).
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000256|ARBA:ARBA00005086}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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DR   EMBL; CP000721; ABR32513.1; -; Genomic_DNA.
DR   RefSeq; WP_011967675.1; NC_009617.1.
DR   AlphaFoldDB; A6LQ83; -.
DR   GeneID; 66343202; -.
DR   KEGG; cbe:Cbei_0325; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_2_0_9; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000000565; Chromosome.
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: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   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABR32513.1}.
FT   DOMAIN          3..181
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          184..280
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         31
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         272
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            138
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   282 AA;  30409 MW;  0AC3B5E9FF86189C CRC64;
     MKKIFVLGAG TMGAGIVQAF AQKGCEVIVR DIKEEFVDRG IAGITKGLEK QVAKGKMSEE
     DKEAILSRIS GTTDMKLAAD CDLVVEAAIE NMKIKKEIFA ELDGICKPEA ILASNTSSLS
     ITEVASATKR PDKVIGMHFF NPAPVMKLVE IIKGIATSQE TFDAVKELSV AIGKEPVEVA
     EAPGFVVNRI LIPMINEASF ILQEGIASVE DIDTAMKYGA NHPMGPLALG DLIGLDVCLA
     IMDVLFTETG DNKYRASSIL RKYVRAGWLG RKSGKGFYDY SK
//
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