ID   A0A285KV50_9ACTN        Unreviewed;       667 AA.
AC   A0A285KV50;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:SNY75727.1};
GN   ORFNames=SAMN05421748_1596 {ECO:0000313|EMBL:SNY75727.1};
OS   Actinoplanes atraurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY75727.1, ECO:0000313|Proteomes:UP000219612};
RN   [1] {ECO:0000313|EMBL:SNY75727.1, ECO:0000313|Proteomes:UP000219612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY75727.1,
RC   ECO:0000313|Proteomes:UP000219612};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBDY01000059; SNY75727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285KV50; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000219612; 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; 2.
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:UP000219612}.
FT   DOMAIN          333..453
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          456..551
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   667 AA;  70953 MW;  000C7055CE33A2BB CRC64;
     MAIHFNREDD GIIVLTFDDP DRAANTMNEA YVRAMQEAVS RLEDERDDVT GVILASAKKS
     WFAGGDLDSL RAYDSAQAAF DRANLVKAQL RRLETLGRPV VAAINGAALG GGLEIALACH
     RRIALPGAQL GCPEVTLGLL PAGGGVVRTV RLLGLTEALT HVLLPGTRHQ AQAALEIGLL
     DQIAASPAEL MSAAREWIRA NPDATQPWES VKVDRTTLPA LPAVLRQRLK GAPYPAPRHI
     LAAAVESTQV DVDTAFVIES RYFAGLVTGH IAKNMISAFF FDRNAANARE IGDLPPPRKA
     AVLGAGMMGA GIAQVLARAG VPVVLRDVDY ERAAAHACDL ITPTADVADL AGADLVIEAV
     FEDPALKHKV FAEIEGVVAP DALLCSNTST LPITALAEGV RRDSDFIGLH FFSPVPKMPL
     VEVIRGEKTS DEALGRALAV VRLLRKTPIV VNDSRGFFTS RVIGTFTNEG VAMLAEGVPP
     ASIEQASSQA GYPAPVLALM DELTLTLPRR IREEALAAGA GTPHPADAVI DRMIDEFGRP
     GRSSGAGFYE YAQGRRVRLW PGLSAFGGTA RPPFDDLKER LLFIEAIETV KCLDEGVLTS
     VAEANIGSIL GIGYPGWTGG VLRYIDQYEG GLPGFVARAR QLAGRYGDRF DPPPLLLAKA
     AEGTTFG
//