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Database: UniProt
Entry: A0A069I6M7_9BURK
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Original site: A0A069I6M7_9BURK 
ID   A0A069I6M7_9BURK        Unreviewed;       717 AA.
AC   A0A069I6M7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KDP85153.1};
GN   ORFNames=CF70_015415 {ECO:0000313|EMBL:KDP85153.1};
OS   Cupriavidus sp. SK-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP85153.1, ECO:0000313|Proteomes:UP000023560};
RN   [1] {ECO:0000313|EMBL:KDP85153.1, ECO:0000313|Proteomes:UP000023560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-3 {ECO:0000313|EMBL:KDP85153.1,
RC   ECO:0000313|Proteomes:UP000023560};
RA   Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT   "Cupriavidus sp. strain SK-3.";
RL   Submitted (MAY-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDP85153.1}.
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DR   EMBL; JFJV02000228; KDP85153.1; -; Genomic_DNA.
DR   RefSeq; WP_035870270.1; NZ_JFJV02000228.1.
DR   AlphaFoldDB; A0A069I6M7; -.
DR   OrthoDB; 5287258at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000023560; 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}.
FT   DOMAIN          320..496
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          499..596
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   717 AA;  76449 MW;  76CDF514B4DC4291 CRC64;
     MKPISVSVDQ DGIALITIDC ADRPVNVYTP ALTAGMSEAV EHVLANDAIV GAIITSGKDG
     FLAGADLNAV LGRLEAALTQ GRSALPGFVA ENLFMRRMET GGKPFAAAIN GTALGGGLEL
     CLACHYRVLS DAPNTRVGLP EVGVGLLPAG GGTQRLPRLL GIEAALPLLL DGTPLAPERA
     LALGVVDEIA PCAELVMRAK RWLLANRGAR QPWDRDGYRL PGGAGALAEH ALRSFHTGIA
     QVRSRTHGNY PAPLAILSAV YEGTQLPFDR GMAIEAQYFA QLAADPVARN LVRTQFVNRK
     RYERLAHRPQ GIPQGAAQRL GILGAGMMGA GIAFAAARAG IEVVLLDATR EQAAAGRLRA
     MEMATRAAVS TTQSEPTQHA GKLIHATAHY GDLDGCDFVI EAVFEDRAVK ADVIARALTV
     LSPTAIFASN TSTLPITSLA TGTGRPERFI GMHFFSPVDR MPLLEIILGE RTSRETLAHA
     MDLAARLRKT PIVVNDSPGF YTSRIFCAYV DEAMAMLAEG VKPALIENAA RMAGMAVSPL
     AVLDEVSLDL QQRVVRQAEA DGVPEPLRRI HAQPVIARMN AIDRLGRKRG GGFYDYPEGG
     RKHLWPGLAQ AYPAARQQPG LEEVKRRLLH VQALESVRCM EEGVISAPED ADIGAILGLG
     FPAWTGGPLS LVDTIGVRAF VLACDALADA YGSRFRPTQA LRERARRGEP FYSKEAA
//
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