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Database: UniProt
Entry: D1C320_SPHTD
LinkDB: D1C320_SPHTD
Original site: D1C320_SPHTD 
ID   D1C320_SPHTD            Unreviewed;       283 AA.
AC   D1C320;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:ACZ38637.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:ACZ38637.1};
GN   OrderedLocusNames=Sthe_1202 {ECO:0000313|EMBL:ACZ38637.1};
OS   Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC   Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC   Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX   NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ38637.1, ECO:0000313|Proteomes:UP000002027};
RN   [1] {ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA   Goeker M., Klenk H.P., Eisen J.A.;
RT   "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ38637.1, ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RX   PubMed=21304676;
RA   Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA   Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Desulfohalobium retbaense type strain
RT   (HR(100)).";
RL   Stand. Genomic Sci. 2:38-48(2010).
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; CP001823; ACZ38637.1; -; Genomic_DNA.
DR   RefSeq; WP_012871684.1; NC_013523.1.
DR   AlphaFoldDB; D1C320; -.
DR   STRING; 479434.Sthe_1202; -.
DR   KEGG; sti:Sthe_1202; -.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_2_0_0; -.
DR   InParanoid; D1C320; -.
DR   OrthoDB; 9771883at2; -.
DR   Proteomes; UP000002027; Chromosome 1.
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; 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:ACZ38637.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002027}.
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         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="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   283 AA;  30621 MW;  CA45E7A4AD82E8F1 CRC64;
     MEITRVAVVG AGTMGSGIVQ VVARAGIPVT MIDRDQAILD RAFETIAQRL HREVEKGRLT
     EEEAGVATSL IQTDASVDSA AEADLVIEAV PEVLDLKADI FRRLDEISPS ATILASNTSS
     ISITQLAAIT RRPDKVVGMH FFNPVPVMQL VEVIRGLGTS DETHAAVMDL ARRLGKTPVT
     VNDFPGFVSN RVLMPMINEA IFCLMEGVAT AEDIDTVMRL GMNHPMGPLA LADLIGLDVC
     LDILEVLHRD LGDDKYRPCP LLRKMVAAGK LGRKTGEGFY TYP
//
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