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Database: UniProt
Entry: A0A248YKP1_9ACTN
LinkDB: A0A248YKP1_9ACTN
Original site: A0A248YKP1_9ACTN 
ID   A0A248YKP1_9ACTN        Unreviewed;       681 AA.
AC   A0A248YKP1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:ASW54195.1};
GN   ORFNames=CIK06_08295 {ECO:0000313|EMBL:ASW54195.1};
OS   Plantactinospora sp. KBS50.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Plantactinospora.
OX   NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW54195.1, ECO:0000313|Proteomes:UP000216795};
RN   [1] {ECO:0000313|EMBL:ASW54195.1, ECO:0000313|Proteomes:UP000216795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS50 {ECO:0000313|EMBL:ASW54195.1,
RC   ECO:0000313|Proteomes:UP000216795};
RA   Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT   "Genome sequencing and analysis of secondary metabolite biosynthetic
RT   capabilities of Plantactinospora sp. KBS50.";
RL   Submitted (AUG-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; CP022961; ASW54195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248YKP1; -.
DR   KEGG; plk:CIK06_08295; -.
DR   OrthoDB; 3216872at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000216795; Chromosome.
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; 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:UP000216795}.
FT   DOMAIN          327..506
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          510..590
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   681 AA;  72982 MW;  A51924B20E6C44AB CRC64;
     MSTDVTYPNE VVTRALLRRV DVPGLDRPAA LITLDNGLDH TKPNTFGPAG LASLDAAIGE
     ALAQRPAFIA VTGKPYIFCV GADITGLPLL RDRDEALEIG RLGHRVFARL RDSEVPTFAF
     VNGAAMGGGL ELALHCHYRT LSGGAAALAL PEVSLGLVPG WGGTQLLPNL IGIPAATQVV
     IQNPLMQNRM LKPRQAAEMG IADVLLEPAD FLERSLEWAA EVVRGAVTVT RPEIDRDMWA
     GVLYFARQTL DERLHGAVPA AYRALDLLET AKDADFATGT AAEDEALADL VFSPELRSGL
     YAFDLVQRRA KRPAGAPDRG LAREVTKVGI VGAGLMASQL ALLFARRLQV PVVLTDLDQA
     RVDKGVGYVH TEIEKAVGKG RMDKGTAAKL YGLVSGSVDR SVFADADFVI EAVFEDLKVK
     KQVWADLEKI VSPEAVLATN TSSLSVTEMA ADLEHPERVV GFHFFNPVAV LPLLEIVRGE
     RTDDATLATA FAVGKQLKKS CVLVKDAPAF VVNRLLTRFL GEIFAAVDAG TPLEVANTAL
     DPLGLPMRPL SLLQLVGPAV AYHVGGTLHA AYPDRFAVSE NLRRIAEAGK PIVVDDKINP
     EAAALLEVGD QPLTAEQVRQ RALDALAQEV RLMLDEGVVA QPQDIDLCLI LGAGWPFHLG
     GITPYLDRAG ISERVTGARF R
//
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