ID A0A0J0YHK6_9FLAO Unreviewed; 295 AA.
AC A0A0J0YHK6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KLT69656.1};
DE EC=1.1.1.157 {ECO:0000313|EMBL:KLT69656.1};
GN ORFNames=AB674_10330 {ECO:0000313|EMBL:KLT69656.1};
OS Flavobacterium sp. ABG.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423322 {ECO:0000313|EMBL:KLT69656.1, ECO:0000313|Proteomes:UP000036173};
RN [1] {ECO:0000313|EMBL:KLT69656.1, ECO:0000313|Proteomes:UP000036173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABG {ECO:0000313|EMBL:KLT69656.1,
RC ECO:0000313|Proteomes:UP000036173};
RA Gimbel A.B., Miller J.R., Newman J.D.;
RT "Flavobacterium sp. ABG.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KLT69656.1}.
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DR EMBL; LEKS01000008; KLT69656.1; -; Genomic_DNA.
DR RefSeq; WP_047776336.1; NZ_LEKS01000008.1.
DR AlphaFoldDB; A0A0J0YHK6; -.
DR STRING; 1423322.AB674_10330; -.
DR PATRIC; fig|1423322.9.peg.2190; -.
DR OrthoDB; 9771883at2; -.
DR Proteomes; UP000036173; Unassembled WGS sequence.
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:KLT69656.1}.
FT DOMAIN 3..182
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 185..281
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 273
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 295 AA; 32019 MW; 978C1C3C4F27900B CRC64;
MKTIAVIGAG TMGNGIAHTF AQSGFVVKLI DVSEKSLDKG MATIAANLDR MQAKGTITPE
EVAKTITNII TYTDIKDGVV GVDLVVEAAT ENVELKLNIF KQLNEACSHN TILATNTSSI
SITQIGAVVA HPERVIGMHF MNPVPIMKLV EIIRGYNTSD EVTKTIMDLS EKLGKTPVEV
NDYPGFVANR ILMPMLNEAI ETLYNKVAGV YEIDTVMKLG MGHPMGPLQL ADFIGLDVCL
AILNVMYEGF KNPKYAPCPL LVNMVRAGKL GVKSGEGFYD YSESKKAEKI SKQFL
//
