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Database: UniProt
Entry: A0A1I2E720_9ACTN
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ID   A0A1I2E720_9ACTN        Unreviewed;       708 AA.
AC   A0A1I2E720;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SFE88503.1};
GN   ORFNames=SAMN05216251_10654 {ECO:0000313|EMBL:SFE88503.1};
OS   Actinacidiphila alni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=380248 {ECO:0000313|EMBL:SFE88503.1, ECO:0000313|Proteomes:UP000199323};
RN   [1] {ECO:0000313|EMBL:SFE88503.1, ECO:0000313|Proteomes:UP000199323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFE88503.1,
RC   ECO:0000313|Proteomes:UP000199323};
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}.
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DR   EMBL; FONG01000006; SFE88503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2E720; -.
DR   STRING; 380248.SAMN05216251_10654; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000199323; 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; -; 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:UP000199323}.
FT   DOMAIN          339..519
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          523..605
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   708 AA;  75195 MW;  D12BDA6FEE5DABAC CRC64;
     MSSTTDLLKG AAERFPDEVV TQAQVRHIEL PGAGRFALIT LDNGFDHTKP TTFGPQSLAN
     LDAAIDQVEK EAAEGTITGV GITGKPFIYA VGADLKGVEV LRTRDEALTI GKSGHDVFKR
     LQTLAVPTFA YYNGAAMGGG VEVGLHCTYR TVSASVPAFS LPEVFLGLVP GWGGCVLLPN
     LIGADRAVGV IIENSLNQNR QLKGAQVYEL GIADALFEAA DFLEQSLAWT AAVLKGELEV
     VRPEVDRGEG WDQAVARGRA IADSKVHGAA PAAYRALDIV AAAKNGDLRH GFDAEDAALA
     DLIMGGELRS GIYAFNLVQK RGKRPVGAPD KALARPVSKV GVVGAGLMAS QLALLFARRL
     EVPVVLTDID QERIDKGVGY VHGEIDKLLA KGRVGQDKAN RLKSLVSGHL DKATAFGDAD
     FVIEAVFEEL GVKQQVFAEL EAVVRPDAIL ATNTSSLSVS EMAAKLEHPE RVVGFHFFNP
     VAVLPLLEIV RGERTDDPSL ATAFAVAKKL KKTAVLVKDA PAFVVNRILT RFMGEIQNVI
     DEGTPVAVAE QAVEPLGLPM SPLVLLELVG PAIGLHVSET LHRAFPDRFT VSENLAAVVK
     AGKRGFYVYD SGKPELDPEV AALLKQGDTV LTEAQVRDRV LDAVAQEIGL MLDEGVVAEA
     QDIDLCLITG AGWPFHLGGI TPYLDREGVS QRVNGKPFLA PGVASVPA
//
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