HBD_CLOAB
ID HBD_CLOAB Reviewed; 282 AA.
AC P52041;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=3-hydroxybutyryl-CoA dehydrogenase;
DE EC=1.1.1.157;
DE AltName: Full=Beta-hydroxybutyryl-CoA dehydrogenase;
DE Short=BHBD;
GN Name=hbd; OrderedLocusNames=CA_C2708;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8655474; DOI=10.1128/jb.178.11.3015-3024.1996;
RA Boynton Z.L., Bennett G.N., Rudolph F.B.;
RT "Cloning, sequencing, and expression of clustered genes encoding beta-
RT hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA
RT dehydrogenase from Clostridium acetobutylicum ATCC 824.";
RL J. Bacteriol. 178:3015-3024(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-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; Evidence={ECO:0000269|PubMed:8655474};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U17110; AAA95971.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK80654.1; -; Genomic_DNA.
DR PIR; C97233; C97233.
DR PIR; T47265; T47265.
DR RefSeq; NP_349314.1; NC_003030.1.
DR RefSeq; WP_010965995.1; NC_003030.1.
DR PDB; 6AA8; X-ray; 2.10 A; A/B/C/D/E/F=1-282.
DR PDB; 6ACQ; X-ray; 2.50 A; A/B/C/D/E/F=1-282.
DR PDBsum; 6AA8; -.
DR PDBsum; 6ACQ; -.
DR AlphaFoldDB; P52041; -.
DR SMR; P52041; -.
DR STRING; 272562.CA_C2708; -.
DR EnsemblBacteria; AAK80654; AAK80654; CA_C2708.
DR GeneID; 44999197; -.
DR KEGG; cac:CA_C2708; -.
DR PATRIC; fig|272562.8.peg.2898; -.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_2_0_9; -.
DR OMA; SVMEVFY; -.
DR OrthoDB; 862072at2; -.
DR BioCyc; MetaCyc:MON-16803; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000000814; 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 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 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Lipid metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..282
FT /note="3-hydroxybutyryl-CoA dehydrogenase"
FT /id="PRO_0000109257"
FT SITE 138
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 130..131
FT /note="RP -> TN (in Ref. 1; AAA95971)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 34..53
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6ACQ"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6AA8"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:6AA8"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:6AA8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6AA8"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:6AA8"
SQ SEQUENCE 282 AA; 30583 MW; E65703B1301F0C6B CRC64;
MKKVCVIGAG TMGSGIAQAF AAKGFEVVLR DIKDEFVDRG LDFINKNLSK LVKKGKIEEA
TKVEILTRIS GTVDLNMAAD CDLVIEAAVE RMDIKKQIFA DLDNICKPET ILASNTSSLS
ITEVASATKR PDKVIGMHFF NPAPVMKLVE VIRGIATSQE TFDAVKETSI AIGKDPVEVA
EAPGFVVNRI LIPMINEAVG ILAEGIASVE DIDKAMKLGA NHPMGPLELG DFIGLDICLA
IMDVLYSETG DSKYRPHTLL KKYVRAGWLG RKSGKGFYDY SK
