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Database: UniProt
Entry: A0A150L109_9BACI
LinkDB: A0A150L109_9BACI
Original site: A0A150L109_9BACI 
ID   A0A150L109_9BACI        Unreviewed;       282 AA.
AC   A0A150L109;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KYD05924.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:KYD05924.1};
DE            EC=1.1.1.35 {ECO:0000313|EMBL:KYD05924.1};
GN   ORFNames=B4102_3097 {ECO:0000313|EMBL:KYD05924.1};
OS   Heyndrickxia sporothermodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD05924.1, ECO:0000313|Proteomes:UP000075666};
RN   [1] {ECO:0000313|EMBL:KYD05924.1, ECO:0000313|Proteomes:UP000075666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4102 {ECO:0000313|EMBL:KYD05924.1,
RC   ECO:0000313|Proteomes:UP000075666};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000256|ARBA:ARBA00005086}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYD05924.1}.
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DR   EMBL; LQYN01000053; KYD05924.1; -; Genomic_DNA.
DR   RefSeq; WP_066231564.1; NZ_LQYN01000053.1.
DR   AlphaFoldDB; A0A150L109; -.
DR   STRING; 46224.B4102_3097; -.
DR   PATRIC; fig|46224.3.peg.3067; -.
DR   OrthoDB; 9771883at2; -.
DR   Proteomes; UP000075666; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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:KYD05924.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT   DOMAIN          4..182
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          185..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         91
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         142
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            139
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   282 AA;  31241 MW;  F68373FDE075D824 CRC64;
     MKRISVIGAG TMGRGIAYTA AVSGFTTILN DISDENLTKA RDYIEKTLET SVKKGFISNT
     TCDEALQNIS YLSDFSESVK EADLVIEAVF ELMELKIDTF KKLDAACPTH TILATNTSTM
     SPTEIAAQTS RPDQCVAMHF FNPVHKMKLI EVVRGLDTSD ETVEKVLEVG RKMDKECVEV
     NEFPGFVTSR MNCLIGNEAM NMLMEGVSSA EDIDKAIKLG LNHPMGPLEL ADLVGLDSRL
     KNMNYLYETL GEKYRPSPLL TKYVKAGRLG RKSGRGFYTY TE
//
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