ID   A0A1G8C2W5_9ACTN        Unreviewed;       696 AA.
AC   A0A1G8C2W5;
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:SDH39735.1};
GN   ORFNames=SAMN05421869_102184 {ECO:0000313|EMBL:SDH39735.1};
OS   Nonomuraea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=633440 {ECO:0000313|EMBL:SDH39735.1, ECO:0000313|Proteomes:UP000199202};
RN   [1] {ECO:0000313|EMBL:SDH39735.1, ECO:0000313|Proteomes:UP000199202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDH39735.1,
RC   ECO:0000313|Proteomes:UP000199202};
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; FNDJ01000002; SDH39735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8C2W5; -.
DR   STRING; 633440.SAMN05421869_102184; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000199202; 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; 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; IPR013328; 6PGD_dom2.
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:UP000199202}.
FT   DOMAIN          335..514
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          518..601
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   696 AA;  73517 MW;  71351188E8452901 CRC64;
     MSELENWRAL LSEHNADEVV TKALVRDVRL PGGAGTMALI TLDNGFDHTK PNTFGAHGLF
     ALNGALSEIA ARTDLAAVGV TGKPFIFAVG ADLTGVAAVT SREQARAVGE LGHHVFRRLA
     ELPIPSFAFV NGAAMGGGLE LALHCDYRTI SAGVPAVALP ECFLGLIPGW GGTQLLPRLI
     GPANAIKLII ENPLSQNRMI KGAQAFELGV ADAMFEPADF LEESLRWAAR VVRGEVTVSR
     PERHDGWAKA VADARFLVDM KLRGASPAPY RALDLIALAE TAGRDEGFAA EDTAIADLLM
     GDEVRAGLYS FDLVQRRAKR PAGAPDASLA RKITKVGIVG AGLMASQMAL LFARRLEVPV
     VLTDLDQVRL DKGVGYVHAE VDKLLGKGRI TADQANRLRS LVTGSLTKDA FADADFVIEA
     VFEDLAVKQQ VFREVEAVVA DTAVLATNTS SLSLTEMGAG LAHPERLVGF HFFNPVAVMP
     LLEIVRGAKT DDATLATAFA VGRSLKKSSV LVKDAPAFVV NRLLTCFMGQ VVAAVDEGTP
     LEVAEHALDG LGLPMTPFAL LQLVGPAVGQ HVAETLHAAF PDRYGLSEGL AKLVAAGKPG
     VYQPDFTLDP EAVALFAGGT TPSTAEQVRE RVLTALATEI RIMLDEGVVA AAQDIDLCMI
     LGAGWPFHLG GITPYLDRTG IAQPRFLAPG VASVPA
//