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Database: UniProt
Entry: A0A0V0RHX0_9BILA
LinkDB: A0A0V0RHX0_9BILA
Original site: A0A0V0RHX0_9BILA 
ID   A0A0V0RHX0_9BILA        Unreviewed;       767 AA.
AC   A0A0V0RHX0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE            EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
DE   Flags: Fragment;
GN   Name=HADHA {ECO:0000313|EMBL:KRX14055.1};
GN   ORFNames=T07_13495 {ECO:0000313|EMBL:KRX14055.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14055.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX14055.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX14055.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616;
CC         Evidence={ECO:0000256|ARBA:ARBA00001391};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188;
CC         Evidence={ECO:0000256|ARBA:ARBA00001391};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC         + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62613; Evidence={ECO:0000256|ARBA:ARBA00000193};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC         Evidence={ECO:0000256|ARBA:ARBA00000193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:31163, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC         ChEBI:CHEBI:62613; Evidence={ECO:0000256|ARBA:ARBA00000469};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165;
CC         Evidence={ECO:0000256|ARBA:ARBA00000469};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU003707}.
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}.
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:KRX14055.1}.
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DR   EMBL; JYDL01000173; KRX14055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0RHX0; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProt.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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; 2.
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.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
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:UP000054630}.
FT   DOMAIN          367..544
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          547..642
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          677..759
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX14055.1"
SQ   SEQUENCE   767 AA;  84507 MW;  BC9F38ED155A8DE7 CRC64;
     LVSDRRMATF FGLTTVARST LSAKFQVLRL CNRCSTNIST LTRMNSYRDE EIGIIKFHTP
     GSKENIMDIN FMMEFYDCLN KFTQDVSIKG IVVMSGKSGS FIAGADTKII ASCHSVAEAT
     ALSLKCQAIM NRIHSNYKPV VAAINGTCLG GGLELALACD YRIAVNSKKT IFGLPEVRLG
     LLPGAGGTQR LPRLISIIDS MDLMLTGKTI SASKAKSIGL VDMLVEPLGP GLHTDEDYMI
     KELEQGAVQV LRDLLSTELV VLRKLKFPHN LVHTLLDIEL FRNLFFVYMR NKVEKSTHGH
     YPAPSHIVNV VRKGYKFGIG DGLKAEAKAF GLVATSPESK SLIHLFTSST ECKKNPFPPV
     KKEPKSLAVI GAGLMGCGIA QVSIYNGFVT YLNDLDKEAL LRGERSIAQH LDKKVKQQSI
     TILEKDNMLA NLFLSVDREA IKNADLLIEA VFEDVELKQK VLREIEQCVR PDCVIASNTS
     AISISKIAEA SERPENIVGM HYFSPVDKMK LLEVITTSKT SKEAASAAVN VGLRQGKFVI
     VVKDSPGFYT TRVLAAMLSE TIRLLQEGVS PKELNDLCIG FGFPVGFVTL VDEVGIDVAL
     HIAKYLGEKL GQRMAGGDIS VLQKMVDNNF LGRKSGKGCF DYSKSKVKQM NSKALQIFKD
     HAKPSRGCDS DHDRQLRMVS RFVNEALLCL EEGVISSPRS GDIGAVFGLG FPPFWGGPFR
     FVDNYGAERL VKEMDRYRDC YGDAAEFQAC QLLRDHANDS KKKFYTI
//
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