ID A8RDP3_9FIRM Unreviewed; 290 AA.
AC A8RDP3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase, NAD binding domain protein {ECO:0000313|EMBL:EDP10749.1};
GN ORFNames=EUBDOL_02012 {ECO:0000313|EMBL:EDP10749.1};
OS Amedibacillus dolichus DSM 3991.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Amedibacillus.
OX NCBI_TaxID=428127 {ECO:0000313|EMBL:EDP10749.1, ECO:0000313|Proteomes:UP000004090};
RN [1] {ECO:0000313|EMBL:EDP10749.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10749.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium dolichum (DSM 3991).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDP10749.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10749.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2007) 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:EDP10749.1}.
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DR EMBL; ABAW02000024; EDP10749.1; -; Genomic_DNA.
DR AlphaFoldDB; A8RDP3; -.
DR STRING; 428127.EUBDOL_02012; -.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_2_0_9; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000004090; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
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}.
FT DOMAIN 14..189
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 192..288
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 19..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT SITE 146
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 290 AA; 31499 MW; A8BAE4A2E7792117 CRC64;
MAFKIIKEIK KMKKVGVIGA GTMGQGIANA FASNGYDVTV CDIKIEWAQG GIDKIAGKMD
KLVAREKMTA EKAAEVKANL KAGVYEDLAD CDLIVEAVLE KMEVKKDLFT KLDEICKDSC
IFGTNTSSLS ITEIATGIKH NVIGMHFFNP ADRMKLVEVI SGINTPVETK EAILEISKSL
GKTPVEVAEG PGFVVNRILI PMINEAAFIL QEGIASVEDI DTAMKLGANH PMGPLALGDL
IGLDIVEAIM DVLYNETKDS KYRCCTLIRK MVRGKKLGQK TGVGFYDYSK
//
