ID A0A0J1BFC3_9SPHI Unreviewed; 298 AA.
AC A0A0J1BFC3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:KLT63798.1};
DE EC=1.1.1.157 {ECO:0000313|EMBL:KLT63798.1};
GN ORFNames=AB669_20375 {ECO:0000313|EMBL:KLT63798.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT63798.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT63798.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT63798.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
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:KLT63798.1}.
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DR EMBL; LECU01000010; KLT63798.1; -; Genomic_DNA.
DR RefSeq; WP_047801200.1; NZ_LECU01000010.1.
DR AlphaFoldDB; A0A0J1BFC3; -.
DR STRING; 1663685.AB669_20375; -.
DR PATRIC; fig|1663685.3.peg.4282; -.
DR Proteomes; UP000036014; 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:KLT63798.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT DOMAIN 5..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 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 32
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 298 AA; 32707 MW; 0C54C31CEE5A58AD CRC64;
MIEAVSIIGS GTMGNGICHL FAQYNFKVNL IDVSQDALNK ALATISRNFD RQIAKGTLTD
DQKIQALEKI TTYTSIKEGV ENADLVVEAA TENLDLKLNI FRDLDQYAPE HCILASNTSS
ISITQIAAVT NRGDKVIGMH FMNPVPVMKL VEVIRGYQSS DETTALIMAL SINLDKIPVE
VNDYPGFVAN RILMPMINEA IYTLYEGVAG VYEIDTVMKL GMAHPMGPLQ LADFIGLDIC
LAILKVLHDG FGNPKYAPCP LLVNMVNAGY KGIKTDEGFY RYTAGSKDLI VSEKFKRS
//
