ID A0A0U5E9V4_9GAMM Unreviewed; 700 AA.
AC A0A0U5E9V4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=THIOKS1680012 {ECO:0000313|EMBL:CRI67555.1};
OS Thiocapsa sp. KS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=610332 {ECO:0000313|EMBL:CRI67555.1, ECO:0000313|Proteomes:UP000198608};
RN [1] {ECO:0000313|Proteomes:UP000198608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|Proteomes:UP000198608};
RA Luecker S.;
RL Submitted (MAY-2015) 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 N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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; CVPF01000338; CRI67555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5E9V4; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000198608; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
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; IPR006180; 3-OHacyl-CoA_DH_CS.
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.
DR PROSITE; PS00067; 3HCDH; 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, ECO:0000313|EMBL:CRI67555.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CRI67555.1}.
FT DOMAIN 322..494
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 498..591
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 700 AA; 76781 MW; 142944456FB0596A CRC64;
MNTLWTIEQD ATDGICRLGI DDRSHSVNLL SVAALDELDA CIARVENGLE TGLATGIEAG
PYPHPIKGLI IQSRKPKGFI AGADVGEFDR LADPSEAERH IRRVHALLAR IEDLPIPTLA
LIHGVCLGGG LELALACRYR IASDDPATKL GFPEVRLGIF PGYGGTWRAI RTLGPVAAMQ
AMLTGQTYSA RQAQRMGLVD RVLPQRQLEA GARDLLRAAP LPSRASFSQR LPNLPAVRGW
VAHRMTRRTA AKVRQEHYPA PFALIEHWRA NGANARGLLD GEARRVPELL LGETSTNLRR
VFHLQERLKA LSDVEVPRPQ RVHVVGAGVM GGDIAAWCAL NGLTVTLQDL SLDQIGRAMK
RAHHLFEQRL RDPRLVRAAW DRLMPDPDGE GLHRTDLVIE AVAEQTELKQ QLFAEMETLI
PEHALLATNT SSIPIERIGE GLRDPGRLVG LHFFNPVARM QLVEVVQGTQ TRPESMQRGL
AAVRALDRLP LPVKSSPGFL VNRVLMPYLL EAVDLLDEGV SIAAIDKAAV DYGMPMGPLA
LADTVGLDIC LAVSDTLGPA LTAPEETPER LRRMVADGQL GKKSGRGFHR YRDGQAVPES
ISHGDRPPHD LTERLIFRLL NECVACLREG VVADPDLLDA GVVFGTGFAP HRGGPLHEIA
QGGWERMRER LDTLQRDHGR HFRPDRGWQL TPAGLYRGGH
//
