ID   A0A1C6UDF6_9ACTN        Unreviewed;       700 AA.
AC   A0A1C6UDF6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SCL52125.1};
GN   ORFNames=GA0070617_1986 {ECO:0000313|EMBL:SCL52125.1};
OS   Micromonospora yangpuensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=683228 {ECO:0000313|EMBL:SCL52125.1, ECO:0000313|Proteomes:UP000198937};
RN   [1] {ECO:0000313|EMBL:SCL52125.1, ECO:0000313|Proteomes:UP000198937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45577 {ECO:0000313|EMBL:SCL52125.1,
RC   ECO:0000313|Proteomes:UP000198937};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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}.
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DR   EMBL; FMIA01000002; SCL52125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6UDF6; -.
DR   STRING; 683228.GA0070617_1986; -.
DR   OrthoDB; 3216872at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000198937; Unassembled WGS sequence.
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; -; 2.
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:UP000198937}.
FT   DOMAIN          326..516
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          520..599
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   700 AA;  74243 MW;  48C86C281203A120 CRC64;
     MSALVAPNEV VTRALLRHVD VPGLDRRAAL ITLDNGHDHT KPNTFGPAGL ASLDEAISAA
     LAADPAFVAI TGKPYIFSVG ADLVGLPALA DRDQALEIGR LGHRIFARLR DSPVPTFAFV
     NGAAMGGGLE LALHCHYRTL SGGATALALP EVFLGLVPGW GGTQLLPNLV GIPAATQVIL
     QNPLTQNKML KPKQAAEMGL ADVLLEPADF LERSLLWAAD VVSGRVTVTR PEVDRDMWAG
     VLYFARQTLD QRLHGAVPAA YRALDLLETA KDADFATGTA AEDEALADLI FSEELRSGLY
     AFDLVQRRAK RPAGAPDKGL ARPVTKVGIV GAGLMAGQLA LLFARRLQVP VVLTDLDQAR
     VEAGVAYVHS QIEKQVTRGR LDKGTAAKMY GLVSGATTAE AFAASTPGQR TSFADCDFVI
     EAVFEDLSVK KQVWAELEKI VSPEAVLATN TSSLSVTAMA ADLEHPQRLV GFHFFNPVAV
     LPLLEIVRGE RTDDATLATA FAVGRQLKKS SVLVSDAPAF VVNRLLTRFL GTVFAAVDAG
     TPLEVANNAL DPLGLPMRPL ALLQLVGPAV AHHVAGTLHE AFPDRFTVSG NLKRIADSGQ
     PIVVDDEINA EVAKLLVVGD QPLTAEQVRQ NALDALAEEI RLMLDEGVVA EAQDIDLCLI
     LGAGWPFHLG GITPYLDRTG TSERVTGRRF LPPGAASLPG
//