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Database: UniProt
Entry: F6DHQ8_THETG
LinkDB: F6DHQ8_THETG
Original site: F6DHQ8_THETG 
ID   F6DHQ8_THETG            Unreviewed;       290 AA.
AC   F6DHQ8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:AEG33679.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:AEG33679.1};
GN   OrderedLocusNames=Ththe16_1276 {ECO:0000313|EMBL:AEG33679.1};
OS   Thermus thermophilus (strain SG0.5JP17-16).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=762633 {ECO:0000313|EMBL:AEG33679.1, ECO:0000313|Proteomes:UP000009233};
RN   [1] {ECO:0000313|EMBL:AEG33679.1, ECO:0000313|Proteomes:UP000009233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG0.5JP17-16 {ECO:0000313|EMBL:AEG33679.1,
RC   ECO:0000313|Proteomes:UP000009233};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA   Gladden J., Woyke T.;
RT   "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000009233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG0.5JP17-16 {ECO:0000313|Proteomes:UP000009233};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA   Gladden J., Woyke T.;
RT   "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000256|ARBA:ARBA00005086}.
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DR   EMBL; CP002777; AEG33679.1; -; Genomic_DNA.
DR   RefSeq; WP_008632695.1; NC_017272.1.
DR   AlphaFoldDB; F6DHQ8; -.
DR   KEGG; tts:Ththe16_1276; -.
DR   PATRIC; fig|762633.3.peg.1265; -.
DR   HOGENOM; CLU_009834_2_0_0; -.
DR   Proteomes; UP000009233; 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:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
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; 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.
PE   4: Predicted;
KW   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEG33679.1}.
FT   DOMAIN          6..183
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          186..282
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         49
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         56
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         119
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   290 AA;  31802 MW;  A49E4A3FAA9CEE2D CRC64;
     MEVKRIGVVG AGQMGSGIAQ VAASAGYEVV LVDVAESFLE RGLAAIRRSL GKFLEKGKIT
     QEAHDEALGR IRTSLSLEDL KEADLIVEAI VEDEGEKRRL FERLGALAKP EAILASNTSS
     IPITALARYS GHPERFIGMH FFNPVPLMQL VEVIRGELTS EATRDVVVEV ARRMGKTPLE
     VQDYPGFISN RLLMPMINEA IEALREGVAT KEAIDGIMRL GMNHPMGPLE LADFIGLDTC
     LAIMEVLHRG FGDDKYRPSP LLRRMVQAGL LGRKVGRGFY TYDEKGNKVG
//
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