ID A0A0K2YKG9_9NOCA Unreviewed; 286 AA.
AC A0A0K2YKG9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:CRK52512.1};
DE EC=1.1.1.157 {ECO:0000313|EMBL:CRK52512.1};
GN ORFNames=RHCRD62_40399 {ECO:0000313|EMBL:CRK52512.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK52512.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK52512.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK52512.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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DR EMBL; CVQP01000007; CRK52512.1; -; Genomic_DNA.
DR RefSeq; WP_050065583.1; NZ_CVQP01000007.1.
DR AlphaFoldDB; A0A0K2YKG9; -.
DR STRING; 260936.RHCRD62_40399; -.
DR OrthoDB; 9771883at2; -.
DR Proteomes; UP000044872; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:RHEA.
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; PTHR43561; -; 1.
DR PANTHER; PTHR43561:SF3; HYDROXYACYL-COENZYME A DEHYDROGENASE, MITOCHONDRIAL; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CRK52512.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000044872}.
FT DOMAIN 6..185
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 190..283
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 143
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 286 AA; 30762 MW; E096529E1C5B7B65 CRC64;
MTAINKVTVL GTGVLGSQIA YQTAYHGVDV VAYDISDEVL DKAKARFAGL AQTYKAEVDG
AADGAADAAL DRIRYSADLA DAVEDADLVI EAIPENLDLK RDTYTKLGEV APAKTIFATN
SSTLLPSDLK GFTGRPEKFL ALHFANHVWR QNTAEVMGTD STDPEVYRRV VDFAAAIGMV
PIEIKKEKAG YLLNSLLVPF LSAAGQLVVD GIAEPEMIDE TWRIGTGAPM GPFQIYDVVG
LTTAYNISAA GDEGQRRFAE YIKENYIDKG KLGAATGEGF YAYSVE
//