ID   A0A1G7C747_9ACTN        Unreviewed;       714 AA.
AC   A0A1G7C747;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SDE35129.1};
GN   ORFNames=SAMN04489747_3183 {ECO:0000313|EMBL:SDE35129.1};
OS   Auraticoccus monumenti.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Auraticoccus.
OX   NCBI_TaxID=675864 {ECO:0000313|EMBL:SDE35129.1, ECO:0000313|Proteomes:UP000198546};
RN   [1] {ECO:0000313|EMBL:SDE35129.1, ECO:0000313|Proteomes:UP000198546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MON 2.2 {ECO:0000313|EMBL:SDE35129.1,
RC   ECO:0000313|Proteomes:UP000198546};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT629688; SDE35129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7C747; -.
DR   STRING; 675864.SAMN04489747_3183; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000198546; Chromosome i.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198546}.
FT   DOMAIN          345..524
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          526..609
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   714 AA;  75375 MW;  E2B9AADC2B6C3E2F CRC64;
     MTTYLPDADL ERLIAEASAL TADDEVVTSA LSRDVALPHG AGTAVLITLD NGLDHTRPNT
     LGPQSMGRLN AAVDAALARA DVAAVAITGK PFILAAGADL SGVAKLTSPE QATAIARIGH
     GVYAKLADAT IPTFCFVNGL ALGGGLEIAL GCHYRTVSAS APAVALPEVF LGLVPGWGGA
     YLLPNLIGPD NAIKVIIENS MNQNRMLQGH QLQGLGIADA TFEAADFLER SLDWAARVVT
     GEVVVERPEP DRGAGWDAAV ARGRAVADAK VHGTAPAPYM ALDLVDAARS RTRDEAFAAE
     DEALTELIMS DELRASLYAF ELVQKRAKRP AGAPDKGLAR PVTSVGVVGA GLMASQLALL
     FVRRLEVPVT MSDLDAERAA KGVGYVHAEL DKLHAKGRLS ADRLNRYKAL VSGTTDQADF
     ADCSFVIEAV FEEIGVKKQV FAELEKHVSP ETVLATNTSS LSVGEMAADL QHPERVVGFH
     FFNPVAVLPL LEVVRGERTD DASLATAFSV SKELKKNAVL VRDTRGFVVN RVLLRMMGEI
     TRAMEEGTPP QVADAAVAPL GLPMSPFVLL QLVGPGVALH VAEVLNAEFG ERFHVSQSMR
     NLVEAGKPGV YDWGSDGQPY VSEETAALLV GGDSASTAEE VRQRVEEALA EEIGLMLAEG
     VVAAPMDIDL CLLLGAGWPF HDGGITPYLD RTGVSERVNG RRFLPPGVAS VPRA
//